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PCNT

Pericentrin (PCNT) is a large coiled-coil protein encoded by the PCNT gene located on chromosome 21q22.3 in humans, serving as a core component of the pericentriolar material (PCM) in centrosomes.^[1] This protein plays a critical role in anchoring microtubule-organizing centers and facilitating proper spindle assembly during mitosis and meiosis, thereby ensuring accurate chromosome segregation and cell-cycle progression.^[2] Mutations in PCNT are associated with severe developmental disorders, including microcephalic osteodysplastic primordial dwarfism type II (MOPDII) and Seckel syndrome type 4, characterized by extreme intrauterine growth retardation, microcephaly, and facial dysmorphism due to disrupted centrosomal integrity and DNA damage response pathways.^[3]^[4] Discovered in the early 1990s through studies on centrosomal proteins in mammalian cells, pericentrin was initially identified in rodent tissues as a high-molecular-weight component essential for microtubule nucleation.^[5] Its human ortholog, PCNT, spans approximately 122 kilobases and produces multiple isoforms via alternative splicing, with the full-length form exceeding 3,000 amino acids and localizing primarily to the centrosome throughout the cell cycle.^[1] Beyond cell division, PCNT interacts with regulatory kinases such as PLK1 and CDK1 to modulate PCM maturation and has been implicated in ciliogenesis and neuronal migration during embryonic development.^[2] Clinically, biallelic loss-of-function variants in PCNT lead to a spectrum of primordial dwarfism phenotypes, with MOPDII being the most severe, often accompanied by vascular complications like moyamoya disease and insulin resistance resembling type 2 diabetes.^[3] Diagnostic confirmation typically involves genetic sequencing, revealing truncating mutations or deletions that abolish protein function, while animal models, such as Pcnt-knockout mice, recapitulate the growth defects and centrosomal abnormalities observed in patients.^[6] Ongoing research explores therapeutic strategies targeting downstream pathways, including ATR kinase signaling, to mitigate the DNA repair deficiencies central to these disorders.^[4]

Gene

Genomic Location

The PCNT gene is located on the long arm of human chromosome 21 at cytogenetic band 21q22.3.^[1] In the GRCh38.p14 primary assembly of the human genome, the gene spans genomic coordinates 46,324,156 to 46,445,769 on the forward strand, encompassing approximately 122 kb of sequence.^[1] This positioning was first mapped through fluorescence in situ hybridization studies identifying the human homolog of the mouse pericentrin gene between marker PFKL and the telomere of 21q. The gene comprises 47 coding exons, with the full structure including up to 48 exons when accounting for non-coding regions in certain transcripts.^[7] Intron-exon boundaries have been precisely defined through high-throughput genomic sequencing projects, such as those underlying the reference assemblies in databases like NCBI and Ensembl, revealing splice sites that support multiple transcript variants.^[1] Promoter regions upstream of the primary transcription start site have similarly been annotated from whole-genome sequencing data, facilitating regulated expression in centrosomal contexts.^[8] PCNT exhibits strong evolutionary conservation across vertebrate species, reflecting its essential role in centrosome function. Orthologs are present in diverse mammals, including the mouse Pcnt gene on chromosome 16, as well as in other vertebrates such as zebrafish (pcnt) and chicken (PCNT), with sequence similarity exceeding 70% in core domains based on comparative genomics analyses.^[1] This conservation underscores the gene's ancient origins, traceable through orthology predictions in resources like Ensembl, which identify over 180 vertebrate orthologs.

Structure and Variants

The PCNT gene features a coding sequence spanning approximately 10 kb, which encodes a protein comprising 3336 amino acids in its primary long isoform (NP_006022.3, from transcript NM_006031.6).^[9]^[2] This coding region is distributed across 47 exons within the gene's overall genomic span of about 122 kb on chromosome 21q22.3.^[4] Alternative splicing of the PCNT pre-mRNA generates multiple transcripts, with two predominant isoforms: the long isoform (PCNT-L) and the short isoform (PCNT-S). The PCNT-L isoform incorporates the full set of coding exons, producing the complete 3336-amino-acid protein essential for centrosomal functions. In contrast, the PCNT-S isoform (NP_001302458.1, from transcript NM_001315529.2) uses an alternate 5' exon and splice junction, resulting in an N-terminal truncation and lack of an internal segment, yielding a 3139-amino-acid protein.^[1] This N-terminal truncation in PCNT-S alters the protein's domain architecture while preserving the C-terminal calmodulin-binding and pericentriolar material-targeting motifs shared between the isoforms.^[2] The PCNT gene harbors various genetic polymorphisms, including single nucleotide polymorphisms (SNPs) documented in databases such as dbSNP. For instance, the intronic SNP rs3788265 (G>T) exhibits a minor allele frequency (MAF) of approximately 0.17 in global populations based on gnomAD genomes data, with higher frequencies observed in East Asian cohorts (MAF ≈ 0.43 in 38KJPN and Korean populations).^[10] These polymorphisms, often located in non-coding regions, contribute to genetic diversity across human populations and are tracked for their allele frequencies in resources like the 1000 Genomes Project, where the T allele MAF is about 0.19.^[10]

Protein

Primary Structure

The pericentrin protein, encoded by the PCNT gene, is characterized by a linear amino acid sequence of 3,336 residues in its full-length isoform (PCNT-L or Pcnt B), yielding a calculated molecular mass of approximately 378 kDa.^[5] This extended polypeptide adopts an elongated architecture dominated by coiled-coil motifs, which enable dimerization and scaffolding functions. Sequence analysis reveals a large central coiled-coil domain spanning roughly 1,500 residues, flanked by non-coiled regions, and a smaller C-terminal coiled-coil domain of about 500 amino acids.^[4] A key structural motif is the pericentrin/AKAP450 centrosomal targeting (PACT) domain, a conserved ~90-amino-acid sequence located near the C-terminus (residues ~3230–3320 in the canonical isoform), which consists of an atypical calmodulin-binding IQ motif followed by a coiled-coil segment.^[11] The N-terminal region includes additional coiled-coil segments that contribute to the protein's overall rod-like shape, while the intervening central area exhibits low sequence complexity and is predicted to form a flexible, unstructured linker, facilitating the protein's adaptability in macromolecular assemblies.^[4] Alternative splicing of the PCNT pre-mRNA generates multiple isoforms, including the shorter PCNT-S (or Pcnt S), which lacks the C-terminal region containing the microtubule-binding PACT domain present in PCNT-L, resulting in a reduced molecular weight of ~220 kDa.^[12] This isoform arises from variants that exclude specific exons encoding the C-terminal extension, altering the protein's domain composition while retaining core coiled-coil elements.^[1]

Post-Translational Modifications

Pericentrin, encoded by the PCNT gene, is subject to several post-translational modifications that fine-tune its centrosomal functions. Phosphorylation is a key regulatory mechanism, particularly during mitosis, where it modulates pericentrin's role in centrosome maturation and microtubule organization. Polo-like kinase 1 (PLK1) phosphorylates pericentrin at serine residues Ser-1235 and Ser-1241 in the C-terminal region, initiating the recruitment of pericentriolar material (PCM) components and ensuring proper spindle pole assembly.^[13] This modification occurs specifically at the onset of mitosis and is essential for pericentrin's scaffolding activity within the PCM. Although direct evidence for CDK1-mediated phosphorylation sites on human pericentrin remains limited, mitotic kinases such as CDK1 contribute to the overall hyperphosphorylation of pericentrin, enhancing its dynamic interactions in the coiled-coil domains inherited from its primary structure. Additionally, pericentrin undergoes separase-mediated cleavage during mitotic exit, which removes associated proteins like CDK5RAP2 from the centrosome and facilitates centriole disengagement, thereby regulating pericentrin's localization post-division. Ubiquitination targets pericentrin for proteasomal degradation, controlling its protein levels to prevent centrosome overduplication and associated pathologies. In model organisms, UBR-box E3 ligases such as Poe promote the ubiquitination and turnover of pericentrin homologs, a mechanism likely conserved in humans where elevated PCNT levels are implicated in diseases like cancer and ciliopathies.^[14] This degradation pathway involves polyubiquitin chains that mark pericentrin for 26S proteasome processing, maintaining steady-state abundance during interphase and mitosis.

Biological Role

Centrosome Organization

Pericentrin serves as a core scaffold protein essential for the assembly and maintenance of the pericentriolar material (PCM) in centrosomes, organizing the localization of microtubule-nucleating components to ensure proper centrosomal function.^[15] Through its interactions with centrioles, pericentrin facilitates the structured recruitment of PCM proteins, creating a matrix that supports microtubule nucleation and anchoring.^[16] The recruitment of pericentrin to centrioles is primarily mediated by its conserved C-terminal PACT (pericentrin-AKAP450 centrosomal targeting) domain, which anchors the protein to the centriole wall and positions its extended N-terminal region outward to form a radial scaffold.^[17] This scaffold directly binds and organizes key PCM constituents, including γ-tubulin ring complexes (γ-TuRCs), thereby enabling the PCM to function as an efficient platform for microtubule assembly.^[18] Depletion studies demonstrate that without pericentrin, γ-TuRC recruitment is severely impaired, leading to disorganized PCM architecture.^[15] During interphase, pericentrin contributes to the establishment of the centrosome as the primary microtubule-organizing center (MTOC), promoting the nucleation and stabilization of microtubules that support intracellular transport and cellular polarity.^[15] Its scaffold integrates PCM components to maintain a compact, functional MTOC capable of generating astral microtubule arrays even in the absence of mitotic activation.^[19] Mathematical modeling of centrosome maturation, based on conserved mechanisms in model organisms and consistent with observations in human cells, highlights pericentrin's role in driving exponential PCM expansion through autocatalytic recruitment kinetics, where bound pericentrin molecules catalyze the addition of further PCM proteins via positive feedback mechanisms.^[20]^[21] These models, often described by rate equations for phase separation or scaffold oligomerization, predict rapid PCM growth initiated by pericentrin anchoring, ensuring timely amplification of microtubule nucleation capacity.^[22] For instance, simulations show that pericentrin-like scaffolds enable droplet-like PCM accumulation, with recruitment rates following exponential dynamics dependent on initial centriole-bound concentrations.^[20]

Cell Division Processes

Pericentrin (PCNT) plays a pivotal role in mitotic progression through its phosphorylation-dependent recruitment to spindle poles. During early mitosis, polo-like kinase 1 (PLK1) phosphorylates PCNT at specific serine residues, such as S1235 and S1241, which facilitates its accumulation at centrosomes and initiates centrosome maturation. This phosphorylation event is essential for the expansion of pericentriolar material (PCM) and the subsequent organization of microtubules into a bipolar spindle, ensuring accurate chromosome segregation. Mutants resistant to PLK1 phosphorylation exhibit defective centrosome maturation and impaired spindle assembly, underscoring PCNT's temporal regulation in mitosis.^[23] PCNT further contributes to spindle formation by interacting with microtubule motors, particularly cytoplasmic dynein, to promote aster formation and centrosome positioning. Through direct binding to the dynein light intermediate chain via its C-terminal region, PCNT anchors dynein at centrosomes, enabling the motor to generate forces that organize astral microtubules and separate centrosomes for bipolar spindle establishment. This interaction is mitosis-specific, as PCNT-dynein complexes localize to spindle poles to nucleate and focus microtubules. Defects in PCNT, such as depletion or mutation, disrupt these interactions, leading to monopolar spindles characterized by failed centrosome separation and disorganized microtubule asters, which compromise mitotic fidelity.^[24]^[25] In cytokinesis, PCNT facilitates abscission by coordinating centrosome disorganization and movement toward the cytokinetic bridge during the pre-abscission phase. PCNT enrichment at the mother centriole, regulated by Rab11 endosome trafficking, drives centrosome reorientation and partial disassembly, which clears the path for midbody constriction and membrane ingression. Impairment of PCNT, as observed in heterozygous mutants, results in delayed centrosome motility, abscission failure, and increased binucleation, highlighting its necessity for completing cell division.^[26]

Developmental Roles

Beyond cell division, PCNT is implicated in ciliogenesis, where it contributes to the formation and function of primary cilia as microtubule-organizing centers in non-dividing cells.^[2] Additionally, PCNT plays a role in neuronal migration during embryonic development by supporting centrosome function in directed cell movement and polarity establishment.^[2]

Clinical Significance

Associated Disorders

Mutations in the PCNT gene are primarily associated with microcephalic osteodysplastic primordial dwarfism type II (MOPDII), a severe form of primordial dwarfism characterized by extreme intrauterine and postnatal growth retardation, profound microcephaly, and distinctive skeletal dysplasia including short stature with an average adult height of approximately 100 cm.^[27] Additional clinical features include facial dysmorphism with a prominent nose and low-set ears, as well as complications such as cerebrovascular anomalies like moyamoya disease and increased risk of aneurysms.^[28] MOPDII was first linked to biallelic loss-of-function mutations in PCNT in 2008, with early reports identifying 29 such mutations across affected families.^[27] Hypomorphic alleles in PCNT can result in milder phenotypes, including isolated microcephaly or variants resembling Seckel syndrome, which feature proportionate short stature, milder microcephaly, and subtle skeletal abnormalities without the full spectrum of MOPDII dysmorphology.^[29] For instance, some patients initially diagnosed with Seckel syndrome have been reclassified under the MOPDII spectrum upon genetic confirmation of PCNT variants, highlighting phenotypic overlap.^[30] PCNT-related disorders follow an autosomal recessive inheritance pattern, requiring biallelic mutations for disease manifestation.^[28] The prevalence is extremely low, estimated at less than 1 in 1,000,000 individuals, reflecting the rarity of reported cases worldwide.^[31] Recent studies as of 2025 have identified novel pathogenic variants in PCNT in patients from diverse populations, such as four Indian pediatric cases, further delineating the genetic heterogeneity.^[32] Examples of pathogenic mutations include frameshift variants such as c.3461_3462del, though detailed molecular analysis is addressed elsewhere.^[27]

Molecular Pathogenesis

Truncating mutations in the PCNT gene, such as nonsense variants, result in loss-of-function alleles that prevent the production of full-length pericentrin protein or produce truncated forms incapable of proper centrosomal targeting.^[33] These mutations abolish pericentrin's localization to the centrosome, disrupting its role as a scaffold for pericentriolar material (PCM) assembly.^[15] For instance, the R2918X nonsense mutation impairs the interaction between pericentrin and Cep57, a key regulator of PCM expansion, leading to disorganized PCM structure during mitosis.^[34] Consequently, PCM fragmentation occurs, characterized by reduced recruitment of PCM components like γ-tubulin, which impairs microtubule nucleation and organization at spindle poles.^[15] This centrosomal dysfunction induces mitotic delays, including prolonged prometaphase and metaphase stages due to spindle assembly defects and chromosome misalignment.^[15] In patient-derived cells harboring PCNT truncating mutations, such as those from Majewski osteodysplastic primordial dwarfism type II (MOPDII), mitotic spindles exhibit fragmentation and asymmetry, triggering checkpoint activation and increased aneuploidy or cell death.^[33] These cellular aberrations reduce overall proliferative capacity, particularly in rapidly dividing tissues, contributing to the disease phenotype at the organismal level.^[15] In the context of neurogenesis, PCNT disruptions diminish the proliferative output of neural progenitor cells, leading to microcephaly through depleted neuronal pools. Mouse models with Pcnt mutations demonstrate reduced brain size, with disproportionate impacts on structures like the olfactory bulb, alongside increased apoptosis and DNA damage in progenitors despite unaltered proliferation rates.^[35] This results in impaired neuronal migration and layering, as evidenced by ectopic interneuron accumulation, ultimately yielding a smaller cerebral cortex with fewer neurons.^[35] Although exact reductions vary, Pcnt-deficient mice exhibit overall brain size decreases observed in severe models, underscoring the role of centrosomal integrity in progenitor expansion.^[35] Systemically, PCNT mutations disrupt endochondral ossification in the growth plates of long bones, contributing to primordial dwarfism. The loss of pericentrin impairs chondrocyte proliferation and differentiation in the hypertrophic zone, leading to disorganized columnar architecture and delayed mineralization.^[33] In MOPDII, this manifests as metaphyseal dysplasia and shortened limbs due to reduced longitudinal bone growth, as truncating variants compromise the mitotic fidelity required for sustained chondrogenesis.^[15]

Interactions

Key Binding Partners

Pericentrin (PCNT) directly binds to CDK5RAP2, a centrosomal protein involved in microtubule organization, through interactions between the central region of PCNT and the C-terminal domain of CDK5RAP2, as demonstrated by co-immunoprecipitation assays in neuronal cells. This binding facilitates the recruitment of CDK5RAP2 to centrosomes, with both proteins featuring multiple coiled-coil domains that likely contribute to their association.^[2] PCNT associates with polo-like kinase 1 (PLK1) during mitosis, where PLK1 phosphorylates PCNT at specific serine residues, including S1235 and S1241, to promote centrosome maturation and pericentriolar material expansion.^[36] These phosphorylation events, identified through in vitro kinase assays and phosphoresistant mutant analysis, are essential for the timely recruitment of other centrosomal components. The C-terminal domain of PCNT mediates direct interactions with components of the γ-tubulin ring complex (γ-TuRC), particularly γ-complex proteins 2 (GCP2) and 3 (GCP3), as confirmed by yeast two-hybrid screens and co-immunoprecipitation.^[37] These bindings anchor γ-TuRCs at spindle poles, supporting microtubule nucleation without direct interaction with γ-tubulin itself.

Functional Networks

Pericentrin (PCNT) plays a central role in the pericentriolar material (PCM) scaffold, anchoring γ-tubulin ring complexes (γ-TuRCs) to centrosomes during mitosis to initiate microtubule nucleation, which is subsequently amplified by the augmin complex for robust spindle assembly.^[38] This integration occurs through PCNT's interaction with γ-tubulin complex proteins (GCPs), ensuring mitosis-specific recruitment of γ-TuRCs to spindle poles and promoting microtubule organization essential for proper chromosome segregation.^[18] Augmin, in turn, binds to these newly nucleated microtubules and recruits additional γ-TuRCs, enabling branching microtubule nucleation that amplifies microtubule density within the mitotic spindle by up to several-fold, as observed in vertebrate cells.^[39] In centrosomal signaling hubs, PCNT facilitates the organization of kinase cascades critical for spindle checkpoint function, particularly through pathways involving Aurora A kinase.^[40] PCNT-dependent recruitment of Cep192 to centrosomes positions Aurora A for autophosphorylation and subsequent activation of Polo-like kinase 1 (Plk1), which drives PCM expansion and microtubule nucleation while contributing to the spindle assembly checkpoint (SAC) by stabilizing Mad2 at unattached kinetochores.^[40] This signaling hub ensures timely mitotic progression, with Aurora A inhibition leading to SAC defects and premature anaphase onset in human cells.^[41] Network analysis using the STRING database reveals PCNT's extensive connections within centrosomal protein families, with top interactors including CEP192 (score 0.999), CEP215 (score 0.998), NIN (score 0.997), CDK5RAP2 (score 0.996), and PLK1 (score 0.995), many of which are centrosomal proteins (CEPs) involved in microtubule organization.^[42] Functional enrichment analysis of the PCNT interactome shows significant overrepresentation of Gene Ontology (GO) terms related to mitosis, such as "mitotic cell cycle" (GO:0000278; FDR 8.3e-3, 5/631 genes) and "microtubule organizing center organization" (GO:0031023; FDR 1.2e-4), underscoring PCNT's embedded role in mitotic regulatory networks.^[42]

References

[1]
5116 - Gene ResultPCNT pericentrin [ (human)] - NCBI
Sep 27, 2025 · The PCNT gene encodes a protein in the centrosome, part of the PCM, important for cell-cycle progression. Mutations cause Seckel syndrome-4 and ...
[2]
PCNT - Pericentrin - Homo sapiens (Human) | UniProtKB | UniProt
Nov 30, 2010 · Pericentrin (PCNT) is a protein involved in microtubule arrays in mitosis/meiosis, and is part of the centrosome and pericentriolar material.
[3]
PCNT gene: MedlinePlus Genetics
Jan 1, 2011 · The PCNT gene provides instructions for making a protein called pericentrin. Learn about this gene and related health conditions.
[4]
Entry - *605925 - PERICENTRIN; PCNT - OMIM - (OMIM.ORG)
Mutations in pericentrin cause Seckel syndrome with defective ATR-dependent DNA damage signaling. Nature Genet. 40: 232-236, 2008.
[5]
PCNT Gene - GeneCards | PCNT Protein | PCNT Antibody
PCNT (Pericentrin) is a Protein Coding gene. Diseases associated with PCNT include Microcephalic Osteodysplastic Primordial Dwarfism, Type Ii and Seckel ...
[6]
Pcnt MGI Mouse Gene Detail - MGI:102722 - pericentrin (kendrin)
Symbol. Pcnt · Name. pericentrin (kendrin) · Synonyms. m239Asp, m275Asp, mKIAA0402, Pcnt2. Feature Type. protein coding gene. IDs. MGI:102722. NCBI Gene: 18541.
[7]
A Novel PCNT Frame Shift Variant (c.7511delA) Causing ... - Frontiers
Jun 24, 2020 · The PCNT gene with 47 coding exons is located on 21q22.3 and covers ~122 kb of genomic sequence (Figure 3A). Moreover, variants in the PCNT gene ...
[8]
https://www.ensembl.org/Homo_sapiens/Gene/Summary?db=core;g=ENSG00000160299
[9]
Homo sapiens pericentrin (PCNT), transcript variant 1, mRNA - Nucleotide - NCBI
- **CDS Length for PCNT Transcript Variant 1**: 10,011 base pairs
[10]
rs3788265 RefSNP Report - dbSNP - NCBI
### Summary of Allele Frequencies for rs3788265 (PCNT Gene)
[11]
The PACT domain, a conserved centrosomal targeting motif in the ...
In this paper we report that AKAP450 and pericentrin share a conserved domain at their C‐termini, outside of their coiled‐coil regions and protein kinase A ...Missing: 1-300 2700-3336
[12]
Pericentrin in health and disease: Exploring the patchwork of ... - NIH
Pcnt is a large coiled-coil protein with so far three known splice variants from orthologous genes in mice and humans. The largest form, Pcnt B, has a ...
[13]
PLK1 phosphorylation of pericentrin initiates centrosome maturation ...
Dec 19, 2011 · PLK1-mediated phosphorylation of pericentrin induces proper organization of the spindle pole–specific pericentriolar matrix and subsequent ...
[14]
The E3 ligase Poe promotes Pericentrin degradation - PubMed - NIH
Aug 1, 2023 · We show that PLP is subject to ubiquitin-mediated degradation and identify multiple proteins that promote the reduction of PLP levels in spermatocytes.
[15]
Pericentrin in cellular function and disease - PMC - NIH
In fact, hypomorphic mutations in the mouse PCNT gene lead to compromised assembly of the olfactory cilia of chemosensory neurons in the nasal olfactory ...Missing: orthologs | Show results with:orthologs
[16]
Pericentrin: Critical for Spindle Orientation - ScienceDirect.com
Oct 6, 2014 · PCNT is a large, elongated coiled-coil molecule that plays a crucial role in centrosome biogenesis and mitotic spindle assembly.Missing: residues | Show results with:residues<|control11|><|separator|>
[17]
The PACT domain, a conserved centrosomal targeting motif in the ...
The PACT domain is a conserved 90 amino acid domain found in AKAP450 and pericentrin, responsible for centrosomal targeting.Missing: PCT | Show results with:PCT
[18]
Mitosis-specific Anchoring of γ Tubulin Complexes by Pericentrin ...
May 14, 2004 · In this study, we show that the centrosomal coiled-coil protein pericentrin anchors γ TuRCs at spindle poles through an interaction with γ tubulin complex ...
[19]
Interphase centrosome organization by the PLP-Cnn scaffold is ...
Jul 6, 2015 · Centrosomes are composed of a pair of centrioles embedded in pericentriolar material (PCM) and function as microtubule (MT) organizing centers ( ...
[20]
Centrosomes are autocatalytic droplets of pericentriolar material ...
In our model, the PCM components exist in two conformations: a form A that dissolves in the cytosol (globular shape) and a form B that segregates from the ...
[21]
Evidence that a positive feedback loop drives centrosome ... - eLife
Sep 9, 2019 · Moreover, a mathematical model that describes centrosome maturation in the early worm embryo treats the centrosome as a liquid, and it is ...
[22]
PLK1 phosphorylation of pericentrin initiates centrosome maturation ...
PLK1 phosphorylation of pericentrin ... Sequential phosphorylation of Nedd1 by Cdk1 and Plk1 is required for targeting of the gammaTuRC to the centrosome.
[23]
Direct Interaction of Pericentrin with Cytoplasmic Dynein Light ... - NIH
The assembly and molecular organization of the centrosome is important for bipolar spindle assembly during mitosis (for review see Waters and Salmon 1997).Missing: PCNT | Show results with:PCNT
[24]
Promoter hijack reveals pericentrin functions in mitosis and the DNA ...
Jan 16, 2013 · Pericentrin is a large PCM protein that is required for normal PCM assembly. Mutations in PCNT cause primordial dwarfism. Pericentrin has also ...
[25]
Rab11 endosomes and Pericentrin coordinate centrosome ... - NIH
Jan 12, 2022 · These studies suggest that Rab11-endosomes contribute to centrosome function during pre-abscission by regulating Pericentrin organization.Rab11 Gtpase Function Is... · Rab11 Gtp-Cycling Mediates... · Pericentrin And Rab11...
[26]
Mutations in the pericentrin (PCNT) gene cause primordial dwarfism
We find that biallelic loss-of-function mutations in the centrosomal pericentrin (PCNT) gene on chromosome 21q22.3 cause microcephalic osteodysplastic ...
[27]
Entry - #210720 - MICROCEPHALIC OSTEODYSPLASTIC ... - OMIM
Majewski osteodysplastic primordial dwarfism type II (MOPD II) syndrome previously diagnosed as Seckel syndrome: report of a novel mutation of the PCNT gene.
[28]
Molecular analysis of pericentrin gene (PCNT) in a series ... - PubMed
The aim of this study was to analyse PCNT in a large series of SCKL-MOPD II cases to further define the clinical spectrum associated with PCNT mutations.
[29]
Mutations in pericentrin cause Seckel syndrome with defective ATR ...
We now report that mutations in the gene encoding pericentrin (PCNT)--resulting in the loss of pericentrin from the centrosome, where it has key functions ...
[30]
Microcephalic osteodysplastic primordial dwarfism type II
Feb 1, 2018 · Mutations in the PCNT gene cause MOPDII. The PCNT gene provides instructions for making a protein called pericentrin. Within cells, this ...
[31]
https://medlineplus.gov/genetics/condition/microcephalic-osteodysplastic-primordial-dwarfism-type-ii/
[32]
https://jmhg.springeropen.com/articles/10.1186/s43042-025-00636-4
[33]
https://doi.org/10.1126/science.1151174
[34]
https://www.nature.com/articles/s41467-019-08862-2
[35]
Mitosis-specific Anchoring of γ Tubulin Complexes by Pericentrin ...
Direct two-hybrid analysis confirmed the interaction of the pericentrin C terminus with both GCP2 and GCP3 (Figure 3E) and failed to detect an interaction with ...
[36]
Multifaceted modes of γ-tubulin complex recruitment and ...
Sep 12, 2023 · Here, we show that Spd-2 recruits γ-TuRCs formed via the GCP4/5/4/6 core, but Cnn can recruit γ-TuSCs directly via its well-conserved CM1 domain.
[37]
The Cep192-Organized Aurora A-Plk1 Cascade Is Essential for ...
Aug 21, 2014 · Our study identifies a Cep192-organized signaling cascade that underlies both centrosome maturation and bipolar spindle assembly.
[38]
Aurora A kinase activity is required to maintain an active spindle ...
Apr 12, 2018 · Aurora A is essential for maintaining the checkpoint protein Mad2 on unattached kinetochores and that inhibition of Aurora A leads to loss of the SAC.
[39]
PCNT protein (human) - STRING interaction network
Active interaction sources: Textmining. Experiments. Databases. Co‑expression. Neighborhood. Gene Fusion. Co‑occurrence. Minimum required interaction score:.Missing: interactome | Show results with:interactome