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Cisterna

A cisterna (plural: cisternae) is a flattened, membrane-bound sac that forms a key structural component of the endoplasmic reticulum (ER) and Golgi apparatus in eukaryotic cells.^[1]^[2] In the ER, cisternae consist of an interconnected network of tubules and sacs that extend throughout the cytoplasm, providing a platform for protein synthesis, folding, and lipid metabolism.^[1] The Golgi apparatus, on the other hand, is organized as stacks of 3 to 20 cisternae, exhibiting polarity with cis (entry) and trans (exit) faces; these facilitate the modification, sorting, and packaging of proteins and lipids received from the ER into vesicles for transport to lysosomes, the plasma membrane, or secretion.^[2] Cisternae are integral to the endomembrane system, enabling the progressive maturation and processing of cellular cargo through mechanisms such as vesicular transport and cisternal progression.^[3]

Structure and Morphology

Definition and Basic Features

Cisternae are flattened, disc-like membrane-bound sacs composed of phospholipid bilayers that serve as intracellular compartments in eukaryotic cells. These structures typically measure 0.5–1.0 μm in diameter and 10–20 nm in thickness, providing a thin, enclosed space for molecular processing.^[4]^[5] The term "cisterna" originates from the Latin word cisterna, meaning "reservoir" or "underground tank," alluding to their role as contained aqueous reservoirs within the cell; the plural form is "cisternae." Unlike spherical vesicles, cisternae are distinguished by their elongated, flattened morphology, which allows for stacked or parallel arrangements to form larger organelles.^[6]^[7] Basic features of cisternae include their potential for smooth or rough surfaces, the latter arising from association with ribosomes on the cytosolic face, and an enclosed aqueous lumen that maintains a distinct internal environment. These sacs can occur in isolated forms or stacked configurations, contributing to the compartmentalization essential for cellular organization as part of the endomembrane system./2:_The_Cell/04:_Cell_Structure/4.4:_The_Endomembrane_System_and_Proteins)^[8]

Locations in Cellular Organelles

Cisternae are prominent features within the endoplasmic reticulum (ER), a network of membrane-enclosed tubules and sacs that extends from the nuclear membrane throughout the cytoplasm.^[1] In the rough ER, these cisternae are studded with ribosomes on their cytoplasmic surface, facilitating protein synthesis and translocation into the lumen.^[9] The rough ER cisternae appear as flattened sacs interconnected by tubules, with ribosomes attached via the cytoskeleton, enabling efficient co-translational modification of nascent polypeptides.^[9] Smooth ER cisternae, lacking ribosomes, form a more tubular and fenestrated network specialized for lipid metabolism, including the synthesis of phospholipids, steroids, and lipoproteins.^[1] These cisternae are abundant in cells engaged in detoxification and hormone production, where enzymes embedded in the membrane catalyze lipid modifications and cholesterol esterification.^[1] Additionally, the perinuclear cisterna represents a specialized ER compartment, defined as the space between the inner and outer nuclear membranes, which is continuous with the rough ER and maintains nuclear integrity while allowing selective transport.^[10] In the Golgi apparatus, cisternae form the structural core as a series of 4-8 stacked, flattened layers per Golgi stack in most mammalian eukaryotic cells, organized into cis, medial, and trans compartments.^[11] These stacks, typically numbering several per cell, are polarized and interconnected by tubules, with the number of cisternae varying slightly by organism but consistently supporting membrane trafficking.^[11] Beyond the ER and Golgi, cisternae appear in specialized forms in other cellular contexts. In skeletal muscle cells, terminal cisternae of the sarcoplasmic reticulum (a specialized smooth ER) flank transverse tubules to form triads, serving as calcium storage reservoirs essential for contraction.^[12] In neuronal soma, hypolemmal cisternae—also known as subsurface cisternae—manifest as smooth ER extensions closely apposed to the plasma membrane, forming membrane contact sites that regulate ion homeostasis and signaling.^[13] For completeness, the cisterna chyli, a dilated lymphatic sac in the retroperitoneum, collects abdominal lymph but represents a non-cellular, extracellular counterpart to cellular cisternae.^[14] The abundance and distribution of cisternae vary markedly by cell type, reflecting functional demands; for instance, secretory cells such as plasma cells exhibit extensively packed rough ER cisternae to accommodate high-volume antibody production.^[15] In contrast, non-secretory cells maintain fewer and more dispersed cisternae, prioritizing other metabolic roles.^[15]

Organization in the Golgi Apparatus

Cis, Medial, and Trans Cisternae

The Golgi apparatus exhibits a pronounced polarity, characterized by its cis, medial, and trans cisternae arranged in a sequential manner within each stack. The cis face, positioned proximal to the endoplasmic reticulum (ER), represents the entry side where nascent cisternae form through the fusion of ER-derived vesicles.^[16]^[4] These cis cisternae initiate the processing pathway. In contrast, the medial cisternae occupy the central region of the stack, facilitating intermediate modifications.^[17]^[18] The trans face, distal to the ER, serves as the exit side, where cisternae mature further before connecting to the trans-Golgi network (TGN).^[16]^[4] This polarized organization ensures a directional flow of cargo through the organelle.^[17] A typical Golgi stack in mammalian cells comprises 3–5 cisternae: one cis, one or two medial, and one trans, forming a compact, plate-like assembly.^[4]^[16] These cisternae are held together by a network of golgin proteins, such as GM130 and giantin, which act as tethering factors, along with GRASP65 and GRASP55 proteins that promote cisternal stacking and fusion.^[4]^[18] The Golgi matrix, composed of proteins, contributes to the structural integrity, creating a ribosome-excluding scaffold that maintains the stack's cohesion.^[4] In many cell types, individual stacks link laterally via tubules to form a ribbon-like Golgi, enhancing overall organization.^[16]^[4] Morphologically, the cisternae display distinct features that reflect their positions. Cis cisternae are often more fenestrated and tubular, with narrow lumens (10–20 nm) and prominent perforations that decrease toward the medial region, aiding initial cargo reception.^[4]^[17] Medial cisternae appear more uniformly flattened with moderate fenestration and fewer associated vesicles.^[4] Trans cisternae, by comparison, are flatter and more compact centrally but exhibit wider rims and increased peripheral fenestration, often with clathrin-coated regions preparing for export.^[4]^[18] The TGN emerges as a specialized extension from the trans face, forming a dynamic tubular and vesicular network with clathrin-coated buds (~100 nm) for sorting cargo into distinct pathways.^[16]^[4] This cisternal stacking is evolutionarily conserved across eukaryotes, appearing similarly in plants, fungi, and animals to support compartmentalized processing.^[19]^[16] Plants feature dispersed stacks with 4–8 cisternae each, maintaining polarity despite mobility along ER networks.^[20] In fungi and animals, the arrangement persists, though variations occur; for instance, budding yeasts like Saccharomyces cerevisiae lack stacked cisternae and instead have scattered individual ones, while yeasts such as Pichia pastoris possess discrete Golgi stacks (typically 2–5 per cell, each with 3–5 cisternae).^[4]^[21] These adaptations highlight the flexibility of the core stacked design.^[18]

Cisternal Maturation and Vesicular Transport Models

The vesicular transport model posits that the Golgi cisternae are stable compartments, with cargo proteins moving anterogradely from cis to trans cisternae via vesicles, while resident enzymes are recycled retrogradely via COPI-coated vesicles to maintain compartmental identity. This model emerged from in vitro reconstitution experiments demonstrating vesicle budding and fusion between Golgi fractions, supporting the idea of discrete transport steps analogous to ER-to-Golgi trafficking.^[22] In contrast, the cisternal maturation model proposes that cisternae themselves are dynamic and transient, progressing from cis to medial to trans faces over time, carrying cargo forward within the maturing cisternae while late-acting enzymes are recycled retrogradely via COPI vesicles to newly forming cis cisternae.^[23] This progression involves the sequential acquisition and loss of enzymatic activities, transforming each cisterna's biochemical environment as it matures.^[24] Live-cell fluorescence microscopy has provided key evidence favoring cisternal maturation, particularly in yeast, where time-lapse imaging revealed individual cisternae disassembling on the trans side and reassembling on the cis side, with cargo remaining associated with progressing cisternae.^[25] In mammalian cells, similar imaging of engineered resident proteins showed dynamic recycling consistent with maturation, though with evidence of supplementary intercisternal continuities like tubules aiding cargo transfer.^[26] Debates persist on the exclusivity of these models, with hybrid mechanisms proposed in plants, where dispersed Golgi stacks exhibit both cisternal progression and vesicular shuttling, as inferred from brefeldin A-induced enzyme redistribution and high-resolution imaging.^[27] The conceptual flow in cisternal maturation follows a cis → medial → trans trajectory, typically spanning 20-60 minutes per stack turnover, allowing efficient cargo modification without extensive vesicular flux.^[24] Microtubules of the cytoskeleton play a critical role in maintaining stack polarity and integrity, anchoring the Golgi ribbon near the centrosome and facilitating directed enzyme recycling to preserve cis-trans orientation.^[28]

Biochemical Functions

Glycosylation Processes

Glycosylation processes in the Golgi cisternae involve the sequential addition and modification of carbohydrate chains to proteins and lipids, transforming precursors from the endoplasmic reticulum into mature glycoconjugates essential for cellular function. These modifications occur across the cis, medial, and trans cisternae, where resident glycosyltransferases and glycosidases ensure compartment-specific processing.^[29] N-Linked glycosylation begins with a mannose-rich oligosaccharide (Man_8-9GlcNAc₂) attached in the endoplasmic reticulum, which enters the cis-Golgi for initial trimming. In the cis and medial cisternae, Golgi α-mannosidase I removes four α1,2-linked mannose residues, reducing the structure to Man₅GlcNAc₂, a committed step for complex glycan formation.^[30] Subsequent additions include N-acetylglucosamine (GlcNAc) by GlcNAc transferase I in the medial cisternae, followed by further mannose trimming by α-mannosidase II; terminal sugars such as galactose and sialic acid are added in the trans cisternae to yield biantennary or triantennary complex glycans.^[29] In contrast, *O*-linked glycosylation initiates primarily in the cis-Golgi with the addition of N-acetylgalactosamine (GalNAc) to serine or threonine residues by polypeptide GalNAc transferases (ppGalNAc-Ts).^[31] Extension occurs progressively: core structures form in the cis cisternae, branching with GlcNAc and galactose proceeds in the medial cisternae, and terminal sialylation or fucosylation completes the chains in the trans cisternae and trans-Golgi network, producing diverse mucin-type glycans.^[31] Lipid glycosylation, particularly of glycosphingolipids, starts with ceramide glucosyltransferase adding glucose in the early Golgi or cis cisternae to form glucosylceramide.^[32] Further elaboration, including lactosylceramide synthesis and addition of galactose, GlcNAc, and sialic acid to create complex structures like gangliosides, takes place in the lumen of the late (trans) Golgi cisternae.^[32] The compartmental specificity of these processes relies on the localization of glycosyltransferases as type II membrane proteins resident in specific cisternae, maintained by recycling via COPI vesicles. For instance, GlcNAc transferase I is primarily confined to the medial cisternae, ensuring ordered modification: trimming in cis/medial, branching in medial, and terminal additions in trans. This sequence—beginning with the endoplasmic reticulum core, followed by cis trimming, medial branching, and trans terminal sugars—prevents premature or incorrect glycosylation.^[33] These glycosylation events are crucial for protein folding, as N-linked glycans interact with calnexin and calreticulin chaperones to guide proper conformation during and after synthesis.^[34] They enhance protein stability by increasing solubility and resistance to proteolysis, while O-linked glycans stabilize folded domains.^[34] Additionally, mature glycans mediate cell recognition through interactions with lectins and adhesion molecules like selectins, facilitating immune responses, cell adhesion, and signaling.^[34]

Phosphorylation, Sulfation, and Proteolytic Cleavage

In the cis cisternae of the Golgi apparatus, phosphorylation occurs primarily through the action of GlcNAc-1-phosphotransferase, which transfers a GlcNAc-1-phosphate group from UDP-GlcNAc to mannose residues on N-linked glycans of newly synthesized lysosomal hydrolases.^[35] This enzyme, consisting of α, β, and γ subunits encoded by GNPTAB and GNPTG genes, initiates the formation of the mannose-6-phosphate (M6P) targeting signal, which is later uncovered by a phosphodiester glycosidase to expose the phosphate for recognition by M6P receptors.^[36] The process ensures proper sorting of lysosomal enzymes to pre-lysosomal compartments, preventing their secretion, and is essential for lysosomal function.^[37] Sulfation in the trans cisternae involves the addition of sulfate groups to tyrosine residues or glycosaminoglycans, catalyzed by tyrosylprotein sulfotransferases (TPST1 and TPST2) using 3'-phosphoadenosine-5'-phosphosulfate (PAPS) as the sulfate donor. This modification enhances protein-protein interactions, such as in coagulation factors or leukocyte adhesion molecules, and occurs specifically in the late Golgi compartments where TPST enzymes are localized.^[38] For glycosaminoglycans, sulfotransferases in the trans Golgi add sulfate to polysaccharide chains, influencing extracellular matrix assembly and signaling.^[39] Proteolytic cleavage takes place predominantly in the trans cisternae and trans-Golgi network (TGN), mediated by furin and other subtilisin-like proprotein convertases that recognize multibasic motifs (e.g., R-X-K/R-R) in precursor proteins.^[40] These endoproteases activate proproteins, such as converting pro-insulin to insulin or processing viral envelope glycoproteins, through site-specific hydrolysis.^[41] Furin, a type I transmembrane protein, cycles between the TGN and endosomes via retrieval signals, ensuring efficient cleavage during secretory pathway transit.^[42] Enzyme compartmentalization in the cisternae is maintained by retrieval signals, such as dilysine motifs (KKXX) for COPI-mediated retrograde transport, which localize phosphotransferases to cis cisternae and sulfotransferases/convertases to trans regions.^[43] Transit timing through the Golgi allows sequential modifications, with total transit time through the Golgi stack estimated at 10-20 minutes based on cargo kinetics in the cisternal maturation model.^[44] These processes yield functional outcomes like enzyme activation, precise targeting signals for lysosomal delivery, and maturation of secretory proteins, distinct from glycosylation events.^[45]

Role in Cellular Trafficking

Integration with the Secretory Pathway

The secretory pathway begins with the export of proteins and lipids from the endoplasmic reticulum (ER) in COPII-coated vesicles, which fuse with the cis face of the Golgi apparatus to initiate processing within the cisternae.^[46] These vesicles bud from ER exit sites and transport cargo anterogradely to the cis-Golgi network (CGN) or early cis cisternae, marking the entry point into the Golgi stack.^[47] Intra-Golgi progression involves the sequential modification of cargo as it moves from cis to medial and trans cisternae, often explained by the cisternal maturation model where cisternae progressively mature while receiving new enzymes via retrograde transport.^[47] Upon reaching the trans-Golgi network (TGN), cargo exits in various vesicles destined for constitutive secretion to the plasma membrane, regulated secretory granules, or transport carriers to endosomes and lysosomes.^[16] Entry into the cis cisternae occurs through the fusion of ER-derived COPII vesicles with target membranes, mediated by SNARE proteins and tethering factors that ensure specificity and directionality.^[46] This fusion event integrates the early secretory pathway with the Golgi, allowing cargo to enter the cisternal lumen for initial glycosylation and quality control.^[48] Retrograde recycling from the Golgi back to the ER, which maintains Golgi resident proteins and retrieves escaped ER components, is facilitated by COPI-coated vesicles budding from cis and medial cisternae.^[46] At the trans face and TGN, cargo is packaged into distinct vesicle types for export, including clathrin-coated vesicles for lysosomal delivery and uncoated or COPI-independent vesicles for plasma membrane targeting via constitutive secretion.^[16] Regulated secretion involves the formation of dense-core granules from the TGN, which store cargo until triggered release, while constitutive pathways enable continuous delivery of membrane proteins and soluble factors.^[49] These exit mechanisms ensure efficient distribution to intracellular destinations or extracellular space, linking the Golgi to the broader endomembrane system.^[49] The total transit time through the Golgi apparatus typically ranges from 10 to 20 minutes for most secretory proteins, allowing rapid processing and export under physiological conditions.^[50] This timescale coordinates with the endomembrane system by synchronizing anterograde flow with recycling loops, preventing bottlenecks and maintaining cellular homeostasis.^[47] Beyond secretion, cisternae exhibit adaptations for non-secretory roles, such as contributing membrane sources to autophagosome biogenesis during autophagy, where trans-Golgi-derived vesicles supply lipids and proteins to forming autophagosomes.^[51]

Protein and Lipid Sorting Mechanisms

In the Golgi cisternae, particularly within the trans-Golgi network (TGN), proteins are directed to specific destinations through recognition of sorting signals by adaptor proteins and receptors. Lysosomal hydrolases bear a mannose-6-phosphate (M6P) signal that binds to M6P receptors in the TGN, facilitating their packaging into vesicles destined for late endosomes and lysosomes.^[16] Certain transmembrane proteins destined for endosomes and lysosomes contain dileucine motifs in their cytoplasmic tails, which interact with adaptor complexes to ensure proper trafficking away from the secretory pathway.^[52] Proteins lacking specific sorting signals follow a default pathway of bulk flow secretion to the plasma membrane, highlighting the selective nature of Golgi sorting mechanisms.^[53] Vesicle formation from cisternae relies on coat proteins that capture cargo based on these signals, followed by SNARE-mediated fusion for specificity at target membranes. Clathrin coats, assembled with the AP-1 adaptor complex, mediate the budding of vesicles from the TGN carrying M6P receptor-bound lysosomal enzymes toward endolysosomes.^[16] Intra-Golgi recycling of resident enzymes and escaped ER proteins occurs via COPI-coated vesicles, which retrieve components from later cisternae back to earlier ones, maintaining compartmental identity.^[16] Fusion of these vesicles with acceptor membranes is ensured by SNARE proteins, whose specific pairing confers targeting fidelity, such as v-SNAREs on vesicles interacting with t-SNAREs on target cisternae or endosomes.^[54] Lipids are sorted within cisternae through lateral segregation into membrane domains, influencing their distribution to distinct cellular destinations. Glycolipids, such as glycosphingolipids, partition into detergent-resistant domains (lipid rafts) in the TGN, directing them preferentially to the apical plasma membrane in polarized epithelial cells, while basolateral sorting involves non-raft pathways.^[55] Cholesterol levels increase progressively toward the trans cisternae, enriching these regions and supporting raft formation for efficient lipid export.^[56] Quality control in the Golgi ensures that misfolded or aberrant proteins are retained or targeted for degradation, preventing their release into the secretory pathway. Misfolded glycoproteins escaping ER quality control are recognized in the Golgi as a distal checkpoint and degraded via proteasomal mechanisms akin to ERAD, involving ubiquitin ligases localized to Golgi membranes.^[57] This process maintains organelle homeostasis by clearing potentially toxic proteins. Dynamic regulation of sorting involves adaptor proteins like GGAs, which are recruited to the TGN by ARF1 and recognize acidic cluster-dileucine signals on cargo, bridging them to clathrin coats for efficient export.^[58]

Biological and Clinical Relevance

Variations Across Cell Types and Organisms

The structure and abundance of Golgi cisternae exhibit significant variations depending on cell type, reflecting adaptations to specific secretory demands. In highly secretory cells, such as pancreatic acinar cells, Golgi stacks typically consist of 4-6 cisternae, enabling efficient processing and packaging of digestive enzymes.^[4] These differences in cisternal number correlate with the overall volume and complexity of the Golgi apparatus, which expands in cells with elevated secretory activity to handle increased cargo flux.^[59] Across organisms, Golgi organization diverges markedly, influencing cisternal architecture and distribution. In mammals, cisternae form polarized stacks of 4-7 flattened membranes, often linked laterally into a continuous ribbon near the centrosome, which facilitates directional cargo progression from cis to trans faces.^[4] Plant cells, by contrast, feature dispersed Golgi stacks scattered throughout the cytoplasm, with each stack comprising 4-6 cisternae that remain unlinked into a ribbon, allowing dynamic positioning near sites of cell wall synthesis and vesicle fusion.^[60] In fungi, particularly yeasts like Saccharomyces cerevisiae, the Golgi typically consists of single, unstacked cisternae that function independently and transit cargo via vesicular shuttling, adapting to the organism's compact cellular architecture.^[61] During cellular development, cisternal organization undergoes dynamic changes to meet evolving functional needs. In B cells differentiating into antibody-secreting plasma cells, the Golgi apparatus expands up to sixfold in volume, with increased cisternal stacking and surface area to accommodate the surge in immunoglobulin production and secretion.^[62] This maturation-driven proliferation of cisternae ensures efficient glycosylation and sorting of antibodies, highlighting the Golgi's plasticity in response to differentiation cues.^[63]

Implications in Disease and Research

Dysfunction in Golgi cisternae has been implicated in several diseases, particularly those involving impaired glycosylation and protein sorting. Congenital disorders of glycosylation (CDG), especially type II subtypes caused by mutations in Golgi-resident glycosyltransferases, lead to defective N- and O-glycosylation, resulting in multisystemic symptoms with prominent neurological manifestations such as hypotonia, seizures, cerebellar ataxia, and developmental delays.^[64] In cystic fibrosis, mutations in the CFTR gene cause mis-sorting of the CFTR protein, exacerbated by Golgi unstacking due to depletion of stacking proteins like GRASP55, which disrupts proper trafficking through the cisternal compartments and impairs chloride channel function in epithelial cells.^[65] Similarly, in cancer, altered sialylation in the trans cisternae, driven by upregulated sialyltransferases localized to medial- and trans-Golgi regions, promotes hypersialylation of cell surface glycans, enhancing tumor cell adhesion, immune evasion, and metastasis to distant organs.^[66] Research on cisternal dynamics has advanced through innovative imaging and genetic tools. Live-cell imaging using GFP-tagged Golgi enzymes, such as mannosidase I for cis cisternae and galactosyltransferase for trans, has visualized cisternal maturation in real time, revealing sequential enzyme progression and cargo transport in yeast and mammalian cells.^[67] CRISPR/Cas9-mediated knockouts of golgins, like GRASP55 and GRASP65, demonstrate that loss of these stacking proteins disperses the Golgi into isolated cisternae and tubulovesicular fragments, accelerating intra-Golgi trafficking while impairing overall stack integrity and protein secretion.^[68] Therapeutic strategies targeting cisternal functions show promise in addressing disease-related defects. Furin inhibitors, which block proteolytic cleavage in the trans-Golgi network, have been shown to prevent maturation of HIV-1 envelope glycoprotein gp160, reducing viral infectivity and production in infected cells.^[69] In diabetes, Golgi processing defects, including dilated cisternae and delayed proinsulin export under hyperglycemic conditions or proinflammatory cytokine exposure, contribute to impaired insulin granule formation and secretion; targeting these disruptions, such as through modulation of Golgi pH or trafficking regulators, represents a potential avenue for improving β-cell function.^[70] Emerging research highlights the Golgi's role in neurodegeneration and leverages post-2000 imaging breakthroughs. In Alzheimer's disease, amyloid-β-induced Golgi fragmentation via cdk5-mediated phosphorylation of structural proteins like GRASP65 promotes tau hyperphosphorylation within cisternal compartments, exacerbating neurofibrillary tangle formation and neuronal dysfunction.^[71] Advances in fluorescence microscopy since 2000, including GFP-based video imaging and super-resolution techniques, have enabled dynamic visualization of cisternal maturation and disassembly, providing insights into Golgi responses to stress and paving the way for high-throughput analysis of therapeutic interventions. Recent studies as of 2025 have identified novel Golgipathies, such as those caused by biallelic variants in GORASP1 leading to glycosylation defects and mitotic issues, and linked Golgi condensation to YAP1 activation in cancer progression. Additionally, Golgi fragmentation has been implicated in dilated cardiomyopathy through dysregulation of structure-maintaining genes.^[72]^[73]^[74]

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Phosphotransferase first acts on acid hydrolases in the endoplasmic reticulum (ER)-Golgi intermediate compartment and continues to transfer GlcNAc-P residues in ...
[44]
Mislocalization of phosphotransferase as a cause of mucolipidosis III ...
Phosphotransferase catalyzes the first step in the generation of the mannose 6-phosphate (Man-6-P) recognition marker on newly synthesized acid hydrolases ...
[45]
The host mannose-6-phosphate pathway and viral infection - PMC
Jan 31, 2024 · The GlcNAc-1-phosphotransferase. GNPT plays a crucial role in initiating the formation of the M6P signal by introducing a phosphate group to ...
[46]
Glycosylation in immune cell trafficking - PMC - PubMed Central
Tyrosine O-sulfation occurs in the trans-Golgi network and is catalysed by two known tyrosyl protein sulfotransferases (Tpst1 and 2) which transfer a sulfuryl ...
[47]
Sulfation affects apical extracellular matrix organization during ... - NIH
Sep 23, 2025 · Sulfation is an abundant post-translational modification that takes place in the Golgi apparatus, where a sulfate group is covalently attached ...
[48]
FURIN AT THE CUTTING EDGE: FROM PROTEIN TRAFFIC TO ...
Abstract. Furin catalyses a simple biochemical reaction – the proteolytic maturation of proprotein substrates in the secretory pathway.
[49]
Two independent targeting signals in the cytoplasmic domain ...
Furin, a subtilisin-like eukaryotic endoprotease, is responsible for proteolytic cleavage of cellular and viral proteins transported via the constitutive ...
[50]
Intracellular trafficking and activation of the furin proprotein convertase
Furin is a membrane-associated endoprotease that efficiently cleaves precursor proteins on the C-terminal side of the consensus sequence, Arg-X-Lys/Arg-Arg1, ...
[51]
Compartmental organization of the golgi stack - ScienceDirect
Brown W.J., Farquhar M.G.. Accumulation of coated vesicles bearing mannose-6-phosphate receptors for lysosomal enzymes in the Golgi region of 1-cell fibroblasts.
[52]
Cargoes move from cis to trans-Golgi compartments and ...
The glycosylation enzymes are distributed in asymmetric gradients within the Golgi apparatus, with early-acting enzymes in the cis-Golgi and the late-acting ...
[53]
Mechanisms regulating the sorting of soluble lysosomal proteins
A recent study suggests that activation by KDELR signaling inside the Golgi also results in lysosomal repositioning, bringing lysosomes close to the perinuclear ...Missing: medial | Show results with:medial
[54]
COPII and COPI Traffic at the ER-Golgi Interface | Physiology
Oct 1, 2011 · This review describes the COPII and COPI coating machineries that generate carrier vesicles and the tethers and SNAREs that mediate COPII ...
[55]
Golgi Compartmentation and Identity - PMC - PubMed Central - NIH
At the final stage, Golgi cisternae produce transport carriers that deliver secretory cargo proteins to plasma membrane domains, regulated secretory granules, ...
[56]
COPI selectively drives maturation of the early Golgi - eLife
Dec 28, 2015 · COPI coated vesicles carry material between Golgi compartments, but the role of COPI in the secretory pathway has been ambiguous.
[57]
A Kinetic View of Membrane Traffic Pathways Can Transcend the ...
Moreover, cisternal maturation may be augmented in some cases by specialized Golgi traffic routes, such as intercisternal tubules in mammalian cells ( ...
[58]
Megavesicles Implicated in the Rapid Transport of Intracisternal ...
Aug 4, 2000 · across the Golgi (which require 10–20 minutes), as was lated ... This transit time is typical of that ob- enclosed aggregate. Such ...
[59]
Golgi Apparatus: A Potential Therapeutic Target for Autophagy ...
Sep 9, 2020 · As a signaling platform, the Golgi provides not only a membrane for autophagosome formation but also a location for induction and elongation of ...
[60]
Ubiquitin-Dependent Lysosomal Membrane Protein Sorting and ...
Feb 5, 2015 · These membrane proteins typically contain an acidic di-leucine targeting motif ... Endosome to Golgi retrieval of the vacuolar protein sorting ...
[61]
Biogenesis of Plant Prevacuolar Multivesicular Bodies - Cell Press
Jan 30, 2016 · At the late Golgi or TGN, soluble proteins without vacuolar sorting signals will be secreted outside of the cell by default. Soluble ...
[62]
SNAREs define targeting specificity of trafficking vesicles by ... - Nature
Apr 8, 2019 · The specificity of vesicle traffic to the Golgi is encoded in the golgin coiled-coil proteins. ... Mechanisms of SNARE proteins in membrane fusion.
[63]
Sorting of GPI-anchored proteins to glycolipid-enriched membrane ...
Abstract. We show that a protein with a glycosylphosphatidyl inositol (GPI) anchor can be recovered from lysates of epithelial cells in a low density, detergent ...
[64]
Cholesterol Regulates Syntaxin 6 Trafficking at trans-Golgi Network ...
Apr 17, 2014 · All together, our data support the hypothesis that cholesterol levels in Golgi and RE membranes fine-tune Stx6 localization and Stx6/VAMP4/VAMP3 ...
[65]
Golgi organization is regulated by proteasomal degradation - Nature
Jan 21, 2020 · A Golgi quality control mechanism has been described as a distal checkpoint to sort aberrant proteins following exit from the ER.
[66]
Single-handed recognition of a sorting traffic motif by the GGA proteins
The mammalian GGAs recognize an acidic- cluster-dileucine signal of the form. (–)–1(D)0X1X2L3L4X5X6. (the subscripted numbers indicate positions relative to the.
[67]
c-Src regulates cargo transit via the Golgi in pancreatic acinar cells
Aug 9, 2018 · Several studies have shown that the Golgi of pancreatic acinar cells is a network of anastomotic, branching elongated ribbon like structures3,4 ...
[68]
GRASPing for consensus about the Golgi apparatus
Apr 13, 2021 · Cultured mammalian cells may possess more than 100 Golgi stacks ... Apparently, the presence or number of GRASP proteins expressed does not ...
[69]
Intra-Golgi transport: A way to a new paradigm? - ScienceDirect
Even though continuities between different cisternae of a Golgi stack have been clearly documented, the question as to whether they are always present at ...
[70]
The Golgi Apparatus and its Next-Door Neighbors - PMC
The Golgi apparatus has been recognized as a central station of intracellular membrane traffic because it stands at the intersection of secretory, lysosomal/ ...
[71]
Organization and Dynamics of the Aspergillus nidulans Golgi during ...
Aug 19, 2009 · EM studies have shown that the Golgi cisternae of filamentous fungi (Howard, 1981; Kurtz et al., 1994; Momany, 2002) and S. cerevisiae (Rambourg ...
[72]
Terminal Cisternae - an overview | ScienceDirect Topics
Terminal cisternae are defined as specialized regions of the sarcoplasmic reticulum that fuse with the transverse tubular system, functioning as sites for ...
[73]
Cell-Autonomous Death of Cerebellar Purkinje Neurons with ...
PCs are unique in having an extensive smooth ER, the “hypolemmal cisternae,” that is “so well developed in PCs that it may be considered a specific ...<|separator|>
[74]
Biogenesis of secretory organelles during B cell differentiation - Kirk
Nov 4, 2009 · In mammalian cell lines, Golgi volume increases in response to Golgi enzyme up-regulation but not in response to increased cargo flux [34].
[75]
XBP1, Downstream of Blimp-1, Expands the Secretory Apparatus ...
The differentiation of B cells into immunoglobulin-secreting plasma cells is controlled by two transcription factors, Blimp-1 and XBP1.
[76]
Congenital Disorders of N-Linked Glycosylation and Multiple ... - NCBI
Aug 15, 2005 · Features include microcephaly, cognitive impairment, seizures, liver abnormalities, recurrent infections, and ectodermal involvement with ...
[77]
New Insights Into the Golgi Stacking Proteins - Frontiers
Jul 15, 2019 · Interestingly, GRASP depletion-mediated Golgi unstacking also causes mis-sorting ... Moreover, GRASP55 binds cystic fibrosis transmembrane ...
[78]
The Distinct Roles of Sialyltransferases in Cancer Biology and Onco ...
SiaTs have been shown to be primarily restricted to medial- and trans-cisternae of the Golgi apparatus, with some being present in the trans-Golgi network ...
[79]
COPI is essential for Golgi cisternal maturation and dynamics
This model is based on the concept that Golgi cisternae progressively change their nature and work as anterograde carriers for secretory protein transport. The ...Results · Discussion · Yeast Strains And PlasmidsMissing: seminal | Show results with:seminal
[80]
Knockout of the Golgi stacking proteins GRASP55 and GRASP65 ...
Oct 15, 2017 · We show that double knockout of GRASP proteins disperses the Golgi stack into single cisternae and tubulovesicular structures, accelerates ...
[81]
Inhibition of Infectious HIV-1 Production by Rerouting the Cellular ...
Jun 5, 2023 · We show that Serpin B8, an endogenous furin inhibitor, can inhibit HIV-1 Env maturation and efficiently reduce infectious HIV-1 production when rerouted to the ...
[82]
Synchronized proinsulin trafficking reveals delayed Golgi export ...
We show that proinsulin trafficking is impeded at the Golgi and coincides with the decreased appearance of nascent insulin granules at the plasma membrane.
[83]
Aβ-induced Golgi fragmentation in Alzheimer's disease enhances ...
Mar 17, 2014 · Here we report that Aβ accumulation triggers Golgi fragmentation by activating cyclin-dependent kinase-5 (cdk5), which phosphorylates Golgi structural proteins ...