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Telophase

Telophase is the final stage of mitosis, the process of eukaryotic cell division that produces two genetically identical daughter cells, during which the separated chromosomes arrive at opposite poles of the cell, the nuclear envelope reforms around each set to create two distinct nuclei, chromatin decondenses from its condensed form, and the mitotic spindle disassembles through depolymerization of microtubules.^[1]^[2] This phase immediately follows anaphase and precedes cytokinesis, the division of the cytoplasm that completes the separation of the daughter cells.^[3] In telophase, nuclear pore complexes reassemble, the nuclear lamina reforms from dephosphorylated lamins, and nucleoli reappear, allowing the resumption of normal nuclear functions such as gene transcription.^[2] Telophase also occurs in meiosis, the specialized cell division that reduces chromosome number for gamete formation, appearing at the end of both meiosis I and meiosis II with similar events of nuclear reformation and chromatin decondensation, though adapted to the haploid products of meiotic division.^[4] In animal cells, telophase overlaps with the initiation of cytokinesis via a contractile cleavage furrow, while in plant cells, a cell plate forms to build the new cell wall.^[1] These coordinated changes ensure accurate distribution of genetic material, maintaining genomic stability across cell generations.^[5]

Overview

Definition and Key Features

Telophase represents the concluding phase of mitosis, occurring immediately after anaphase, during which the separated sister chromatids, having arrived at opposite poles of the cell, and the cellular machinery initiates the reversal of earlier mitotic modifications to restore the interphase configuration.^[6] This stage marks the transition from active chromosome segregation to the reestablishment of nuclear structures, with the two sets of chromosomes beginning to decondense as they cluster at the spindle poles.^[1] Key morphological features of telophase include the reformation of two distinct daughter nuclei, characterized by the reassembly of nuclear envelopes around each chromosome cluster and the reappearance of nucleoli.^[1] Chromosome movement ceases once the chromatids have reached their destinations, and the mitotic spindle begins to disassemble, while preparations for cytokinesis commence; in animal cells, this is evident by the formation of a cleavage furrow that indents the plasma membrane.^[7] These visible changes signify the cell's progression toward completing nuclear division. Functionally, telophase ensures the restoration of nuclear integrity by enclosing the genetic material within reformed nuclei, thereby safeguarding the chromosomes before the final separation of daughter cells via cytokinesis.^[6] This process is essential for maintaining genomic stability, as it prepares each nascent cell for independent interphase activities, including DNA replication and gene expression.^[8] The morphological and dynamic aspects of telophase were first described in 1882 by German anatomist Walther Flemming as part of his pioneering observations on mitotic stages in animal cells, where he detailed the longitudinal splitting and redistribution of chromosomes.^[9]^[10]

Position in Mitosis

Telophase constitutes the concluding phase of mitosis in eukaryotic cells, positioned as the fifth stage in the canonical sequence of prophase, prometaphase, metaphase, anaphase, telophase, and the subsequent cytokinesis. This ordering ensures the orderly segregation and reformation of genetic material prior to cytoplasmic division, with telophase initiating immediately upon the completion of anaphase B, when the separated sister chromatids have fully migrated to the spindle poles. The transition from anaphase is marked by a notable slowing of spindle elongation, signaling the shift from active chromosome movement to nuclear reorganization.^[11]^[12]^[13] In typical mammalian cells, telophase is a brief phase that allows for the essential reversal of earlier mitotic configurations. This duration facilitates the timely progression to cytokinesis, with telophase overlapping the initial stages of cytoplasmic partitioning while concluding once the daughter nuclei are fully reformed and functional. In certain organisms, such as plants, telophase lacks a sharply distinct boundary due to the constraints imposed by rigid cell walls, where the concurrent formation of a cell plate during nuclear reformation blurs the phase's demarcation from cytokinesis.^[6]^[7] The timing and length of telophase exhibit variations across cell types, reflecting adaptations to proliferative demands; for instance, it is shorter in rapidly dividing embryonic cells compared to more protracted durations in somatic cells, optimizing division rates during early development. Prokaryotes, such as bacteria, lack a telophase equivalent altogether, as their reproduction occurs via binary fission without the structured phases of eukaryotic mitosis.^[14]^[15]

Molecular Regulation

Inactivation of Mitotic Cyclin-Dependent Kinases

The cyclin B-Cdk1 complex serves as the master mitotic kinase, driving the progression from prophase through anaphase by phosphorylating numerous substrates that promote chromosome condensation, nuclear envelope breakdown, and spindle assembly.^[16] Its hyperactivation is essential for maintaining the mitotic state, but inactivation is a critical prerequisite for entering telophase and exiting mitosis.^[17] Inactivation occurs primarily through ubiquitin-mediated proteasomal degradation of cyclin B, orchestrated by the Anaphase-Promoting Complex/Cyclosome (APC/C), an E3 ubiquitin ligase. In late mitosis, APC/C is activated by its coactivator Cdh1 (also known as Fzr in some organisms), which replaces the earlier coactivator Cdc20 to target cyclin B for destruction, resulting in an abrupt drop in Cdk1 activity.^[18] This Cdh1-dependent mechanism ensures specific and efficient degradation of mitotic cyclins, distinguishing it from the partial cyclin B breakdown initiated by APC/C-Cdc20 during anaphase onset.^[19] Degradation of cyclin B begins in late anaphase following the separation of sister chromatids and becomes fully effective by early telophase, preventing premature mitotic exit and coordinating the transition to interphase.^[20] This timing is tightly regulated to avoid disruptions in chromosome segregation or cytokinesis. The resulting low levels of Cdk1 activity permit the reversal of mitotic phosphorylations by enabling phosphatase action, thereby distinguishing telophase from the high-Cdk1 phases of earlier mitosis.^[17]

Dephosphorylation of Cdk Substrates

The dephosphorylation of cyclin-dependent kinase 1 (Cdk1) substrates represents a critical step in telophase, reversing the phosphorylations that drive mitotic events and enabling the restoration of interphase cellular architecture. Following the inactivation of Cdk1, primarily through ubiquitin-mediated degradation of mitotic cyclins, protein phosphatases such as Cdc14 in budding yeast and PP2A-B55 in mammalian cells become activated to selectively target these sites.^[21]^[22] In yeast, Cdc14 is released from the nucleolus during the anaphase-telophase transition via the Cdc fourteen early anaphase release (FEAR) network, which involves proteins like Sep12 and Slk19, followed by full activation through the mitotic exit network (MEN) involving Tem1 and Cdc15; this spatial regulation ensures timely dephosphorylation of Cdk1 substrates such as nucleolar proteins and spindle components.^[23] In mammals, an analogous process occurs where inhibition of the Greatwall kinase (MASTL) by declining Cdk1 activity relieves suppression of PP2A-B55, allowing its recruitment to chromatin and central spindle for substrate access during telophase.^[24] These phosphatases exhibit specificity for Cdk consensus motifs, such as (S/T)P sites, on key telophase-relevant substrates including lamins, condensins, and Aurora B kinase. For instance, dephosphorylation of lamin B at Cdk1 sites (e.g., Ser395 in humans) by PP2A-B55 promotes its polymerization and integration into the reforming nuclear lamina, facilitating nuclear envelope reassembly around decondensing chromosomes.^[25] Similarly, reversal of Cdk1 phosphorylation on condensin I and II subunits, such as CAP-D3 and NCAP-H, by PP2A-B55 disrupts their chromatin-binding affinity, contributing to the disassembly of the mitotic chromosome scaffold.^[26] On Aurora B, dephosphorylation of Cdk1 sites (e.g., Thr232 auto-activation loop indirectly influenced) by PP2A-B55 and PP1 cooperates to relocate the chromosomal passenger complex from centromeres to the midbody, silencing its mitotic kinase activity and preventing premature cytokinesis defects.^[27] A hallmark example of substrate-specific reversal is the dephosphorylation of histone H3 at Ser10 by PP1 and PP2A-B55, which begins in late anaphase and completes in telophase, directly initiating chromatin decondensation by alleviating the compact mitotic state and allowing access for interphase factors like RNA polymerase II.^[28] This event is temporally coordinated, with Ser10 dephosphorylation ceasing just prior to visible chromosome relaxation, underscoring its role in precise mitotic exit.^[29] Genome-wide phosphoproteomics in human cells has identified over 16,000 phosphorylation sites, with approximately 9.5% significantly dephosphorylated during early mitotic exit through these phosphatases, including selective reversal of non-Cdk sites initially, followed by Cdk-dependent sites (consensus (S/T)P motifs) on key substrates to ensure resetting of the proteome for G1 entry and preventing aneuploidy.^[30]

Additional Mechanisms Driving Telophase

Beyond the core anaphase-promoting complex/cyclosome (APC/C)-mediated ubiquitination, additional E3 ubiquitin ligases play crucial roles in telophase by targeting residual mitotic kinases for degradation, thereby ensuring the complete silencing of the spindle assembly checkpoint (SAC). SCF complexes, such as SCF^{FBXL2} and SCF^{FBXW7}, specifically ubiquitinate Aurora B kinase, a key component of the chromosomal passenger complex (CPC), promoting its proteasomal degradation at the midbody during late mitosis and telophase. This degradation prevents persistent SAC signaling, which could otherwise delay mitotic exit and cytokinesis. Similarly, SCF complexes facilitate the turnover of Aurora A through interactions involving eEF1A2 and GSK3β, reducing its activity as cells transition to G1 phase. These mechanisms complement APC/C activity by addressing kinase pools not fully cleared by the primary pathway, maintaining irreversible commitment to telophase progression. Calcium signaling pathways, often mediated by calmodulin-dependent processes, coordinate the spatiotemporal dynamics of nuclear envelope reformation with spindle disassembly in telophase. Intracellular calcium transients during anaphase-telophase trigger the association of calcium-binding proteins like annexin 11 with the reforming nuclear envelope, facilitating membrane vesicle fusion and lamina reorganization around decondensing chromosomes. Calmodulin, activated by these calcium waves, modulates actin-myosin interactions that support envelope sealing while integrating with microtubule depolymerization signals from the spindle. Such pathways ensure synchronized remodeling, preventing errors in nuclear integrity that could arise from uncoordinated spindle-envelope interactions. These calcium-calmodulin events are particularly evident in systems like sea urchin embryos, where they link checkpoint resolution to post-mitotic architecture. Recent studies have illuminated novel regulatory mechanisms in telophase, highlighting the dynamic reorganization of chromatin domains. Microcompartments—small, phase-separated nuclear structures—emerge in prometaphase and strengthen progressively through anaphase and telophase, stabilizing chromatin before dilution in G1; this process is influenced by chromatin compaction and opposed by loop extrusion activity. Concurrently, loop-extruding proteins such as cohesin actively rebuild interphase chromatin loops post-telophase, as quantified by super-resolution imaging in human cells, restoring topologically associating domains essential for gene regulation. These advances underscore how telophase serves as a critical window for epigenetic memory preservation via structural reinforcement. Feedback loops involving the inhibition of polo-like kinase 1 (Plk1) further safeguard telophase by preventing reactivation of mitotic entry signals. Dephosphorylation of Plk1 at Thr210 by protein phosphatase 2A-B55 (PP2A-B55), often in coordination with ENSA-mediated regulation, inactivates the kinase during mitotic exit, disrupting its positive feedback with Aurora A and cyclin-dependent kinase 1 (CDK1). This inactivation is integrated with ubiquitin pathways, as SCF-mediated degradation of Plk1 stabilizers enhances phosphatase access, forming a robust barrier against premature G2/M re-entry. Such loops ensure unidirectional progression through telophase, minimizing risks of genomic instability.

Cellular Remodeling Events

Mitotic Spindle Disassembly

During telophase, the mitotic spindle undergoes structural breakdown primarily through the depolymerization of its microtubules, which shortens kinetochore and astral fibers. This process is promoted by microtubule catastrophe-inducing factors such as stathmin (also known as Op18), whose dephosphorylation at mitotic exit activates its ability to destabilize microtubule plus ends, facilitating rapid disassembly.^[31] Concurrently, katanin, an ATP-dependent microtubule-severing enzyme, cleaves microtubules internally, generating shorter fragments that depolymerize more efficiently and contribute to the overall shortening of spindle fibers.^[32] These mechanisms ensure the timely recycling of tubulin subunits, which are repurposed for interphase microtubule networks essential for cellular architecture and motility.^[33] Inactivation of motor proteins further drives spindle disassembly by detaching them from microtubules. Dynein and various kinesins, which maintain spindle integrity during earlier mitotic stages, lose their associations following the relocation of Aurora B kinase from kinetochores to the spindle midzone and subsequent dephosphorylation events that alter their binding affinities.^[34] Aurora B, through its phosphorylation of microtubule-associated proteins, initially supports spindle function but contributes to disassembly by promoting depolymerization once relocated, while kinesin-8 family members actively slide microtubules apart to accelerate breakdown.^[33] The timeline of spindle disassembly begins in late anaphase with initial microtubule shortening and motor detachment, progressing to near-complete dissolution by mid-telophase, allowing the cell to transition efficiently to interphase.^[34] This sequence is conserved in many eukaryotes but varies in plant cells, where full spindle disassembly does not occur; instead, residual spindle elements reorganize into the phragmoplast, a microtubule array that guides cell plate formation during cytokinesis.^[35]

Nuclear Envelope Reassembly

During telophase, the nuclear envelope (NE) reforms around the decondensed chromosomes through a coordinated process involving membrane recruitment, lamina reconstruction, and pore complex reestablishment, restoring nuclear integrity and transport competency.^[36] This reassembly begins as the endoplasmic reticulum (ER)-derived membrane fragments, fragmented during prometaphase, are recruited to the chromatin surface, providing the lipid bilayers essential for the double-membrane structure of the NE.^[37] The initial step in NE reformation entails the fusion of ER membrane vesicles around the chromatin, facilitated by specific protein complexes that bridge membranes to decondensing chromosomes.^[38] Barrier-to-autointegration factor (BAF), a DNA-binding protein, plays a pivotal role by binding to chromatin and recruiting inner nuclear membrane proteins, thereby stabilizing initial membrane attachments.^[39] Subsequently, endosomal sorting complex required for transport-III (ESCRT-III) complexes drive membrane fusion and sealing of gaps in the reforming envelope, ensuring a continuous barrier around the daughter nuclei.^[40] These ESCRT-III-mediated events, often in coordination with BAF, prevent chromatin exposure to cytoplasmic components and promote efficient enclosure, with vesicle fusion occurring progressively from the chromatin periphery inward.^[41] Parallel to membrane recruitment, the nuclear lamina scaffold reassembles via polymerization of dephosphorylated lamin proteins.^[26] Lamins A/C and B, hyperphosphorylated by cyclin-dependent kinase 1 (Cdk1) during mitosis to facilitate disassembly, undergo dephosphorylation primarily by protein phosphatase 1 (PP1) during telophase.^[42] Repo-Man, a chromatin-targeting subunit of PP1, directs this dephosphorylation to specific sites on lamins A/C (e.g., Ser22), enabling their rapid association with chromatin and subsequent head-to-tail polymerization into intermediate filaments that support the inner nuclear membrane.^[43] Lamin B, dephosphorylated similarly by PP1, integrates into the lamina earlier, providing structural stability, while A/C lamins contribute to long-term nuclear architecture.^[44] This ordered reassembly ensures mechanical robustness and proper positioning of nuclear components. Concomitantly, nuclear pore complexes (NPCs) reform to reinstate selective nuclear transport by the end of telophase.^[45] Nucleoporins, dispersed during mitotic disassembly, reassemble in a hierarchical manner, with scaffold nucleoporins like the Nup107-160 complex initiating pore scaffold formation on the reforming membrane.^[46] Nup153, a key nucleoporin at the nuclear basket, is essential for recruiting additional components and stabilizing NPC insertion into the double membrane, facilitating the curvature and fusion required for functional pores.^[47] By late telophase, thousands of NPCs are operational, allowing resumption of nucleocytoplasmic trafficking and signaling essential for G1 progression.^[36] Recent advances have elucidated nanoscale dynamics of ER remodeling during NE reassembly, highlighting how ER membrane curvature is induced by proteins such as Vap33 (in coordination with Ankle2/PP2A) to promote BAF dephosphorylation and efficient vesicle fusion around chromatin.^[48] Such insights underscore the interplay between membrane biogenesis and chromatin templating, with quantitative mapping showing two distinct NPC assembly pathways—one post-mitotic and one interphase—enhancing overall efficiency.^[46]

Chromosome Decondensation

Chromosome decondensation during telophase marks the reversal of mitotic compaction, restoring the chromatin to its interphase configuration to enable gene expression and nuclear function. This process involves the progressive uncoiling of highly condensed mitotic chromosomes, which are approximately 700 nm in width, into thinner interphase threads of about 300 nm. The decondensation is orchestrated by the inactivation and removal of condensin complexes, which had driven the looping and compaction during prometaphase. Specifically, dephosphorylation of condensin I and II subunits by phosphatases such as PP1 promotes their dissociation from chromatin, allowing the looped fibers to relax and unwind.^[25]^[49] Concomitant with condensin release, histone modifications undergo targeted reversals that enhance nucleosome mobility and chromatin accessibility. Phosphorylation of histone H3 at sites such as Ser10, Thr3, and Ser28, which stabilizes condensed structures during mitosis, is actively removed by protein phosphatase 1 gamma (PP1γ) in complex with Repo-Man and Ki-67 during late anaphase and telophase. This dephosphorylation facilitates the reacetylation of histone H4, particularly at lysine 16 (H4K16ac), which neutralizes positive charges on the histone tails and promotes a more open chromatin conformation conducive to decondensation.^[49]^[25] At the topological level, decondensation restores higher-order chromatin organization, including the reestablishment of topologically associating domains (TADs), which are crucial for spatial gene regulation. This occurs through the reloading of cohesin complexes onto chromatin during telophase and early G1, facilitated by the loading factor NIPBL, which replaces the departing condensin to mediate loop extrusion and domain insulation. Cohesin reloading ensures the formation of stable TAD boundaries, often anchored by CTCF, thereby resuming compartmentalized gene expression that was silenced in mitosis.^[50]^[51] Recent advances in imaging have provided quantitative insights into these dynamics. Super-resolution microscopy studies from 2025 reveal that the transition from condensin- to cohesin-dominated genome architecture post-telophase occurs over approximately 2 hours in human cells, with initial binding of about 2-3 cohesin-STAG1 and 5 CTCF molecules per megabase in early G1, scaling up to 8 cohesin complexes per megabase by late G1 to form nested loops and compact TADs. Complementing this, nanoscale DNA tracing techniques have visualized the self-organization of chromatin, showing how mitotic rosette-like structures—characterized by 6-8 Mb overlapping loops extruded by condensin—reconfigure into distinct interphase chromosome territories through stochastic loop repulsion and cohesin-mediated extrusion, with no evidence of helical regularity.^[52]^[53]

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