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Molecular Factors Affecting Cell Division01:27

Molecular Factors Affecting Cell Division

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Several external and internal factors influence the initiation and inhibition of cell division. For instance, the death of nearby cells or the release of human growth hormone (hGH) promotes cell division. In contrast, lack of hGH or crowding of cells can inhibit cell division.
Several proteins function as internal regulators to ensure each cell cycle stage is completed faithfully before proceeding to the next. Regulator molecules may act directly or influence the activity or production of other...
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The stepwise destruction of specific proteins is necessary for the progression and completion of the cell cycle. Such proteins are ubiquitinated by ubiquitin ligases and then subsequently destroyed by the proteasome. The SCF (Skp1/Cullin/F-box) and the anaphase-promoting complex (APC) are two important ubiquitin ligases involved in cell cycle progression. While SCF is active throughout the cell cycle, APC gets activated during metaphase to anaphase transition. Cdc20 or Cdh1 binds to APC and...
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Separation of Sister Chromatids02:17

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At the transition from prophase to metaphase, there is a reduction in cohesion along the chromosomal arms, resulting in the resolution of sister chromatids. However, residual cohesin connections remain to hold the sister chromatids together until the transition from metaphase to anaphase. The residual connection prevents any premature separation of sister chromatids, blocking the risks of aneuploidy within the daughter cells.
At the onset of anaphase, separase, a proteolytic enzyme, is...
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The Contractile Ring02:15

The Contractile Ring

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Contractile rings are composed of microfilaments and are responsible for separating the daughter cells during cytokinesis. Contractile ring assembly proceeds along with other cell cycle events; however, very few mechanistic details are known about the timing and coordination of the contractile rings with the cell cycle.
A small GTPase, RhoA, controls the function and assembly of the contractile ring. RhoA belongs to the Ras superfamily of proteins. The activation of formins by RhoA promotes...
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Rab Cascades01:25

Rab Cascades

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Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.
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Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
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Related Experiment Video

Updated: Nov 18, 2025

Examination of Mitotic and Meiotic Fission Yeast Nuclear Dynamics by Fluorescence Live-cell Microscopy
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Examination of Mitotic and Meiotic Fission Yeast Nuclear Dynamics by Fluorescence Live-cell Microscopy

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Rab14/MACF2 complex regulates endosomal targeting during cytokinesis.

Paulius Gibieža1, Eric Peterman2, Huxley K Hoffman3

  • 1Laboratory of Cell Culture, Institute of Cardiology, Lithuanian University of Health Sciences, Kaunas LT-50162, Lithuania.

Molecular Biology of the Cell
|February 10, 2021
PubMed
Summary

This study investigated the role of Rab14 in cytokinesis, the process by which a cell divides into two. Researchers found that Rab14 helps regulate the targeting of endosomes to the intracellular bridge during cell division. Depletion of Rab14 caused cytokinesis failure or prolonged division time. The study also showed that Rab14 interacts with the MACF2/CAMSAP3 complex, which is involved in microtubule minus-end interactions. This interaction appears to influence how endosomes are localized at the cleavage furrow. The findings suggest that Rab14 and MACF2/CAMSAP3 play a role in actin clearance and endosome targeting during cytokinesis. The study did not establish whether Rab14 is essential for microtubule dynamics. These results provide new insights into the mechanisms that regulate cell division.

Keywords:
Rab14endosome targetingcytokinesiscell divisionmicrotubule dynamics

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Area of Science:

  • Cellular biology
  • Mitotic division mechanisms
  • Endocytic pathway regulation

Background:

Cytokinesis involves precise coordination of actin and microtubule dynamics to complete cell division. Prior research has shown that endosomes containing Rab11 and Rab35 play a key role in this process. However, the mechanisms by which these endosomes are targeted to the cleavage furrow remain unclear. No prior work had resolved the role of Rab14 in this context. This gap motivated an investigation into whether Rab14 contributes to cytokinesis. The study aimed to determine if Rab14 influences endosome localization and actin clearance. Researchers needed to assess how Rab14 depletion affects division time and abscission. Understanding this could clarify how endosomes are regulated at the intracellular bridge. The study focused on identifying new regulators of cytokinesis.

Purpose Of The Study:

The goal was to determine if Rab14 influences cytokinesis by regulating endosome targeting. Researchers wanted to assess how Rab14 depletion affects division time and abscission. They aimed to clarify the role of Rab14 in recruiting Rab11-endosomes to the intracellular bridge. The study sought to determine if Rab14 affects actin clearance at the abscission site. Understanding this could help explain how endosomes are localized during cell division. The researchers also wanted to identify if Rab14 interacts with the MACF2/CAMSAP3 complex. They aimed to test whether this interaction influences endosome targeting. The study focused on uncovering a new regulatory mechanism for cytokinesis.

Main Methods:

The researchers used depletion experiments to assess the role of Rab14 in cytokinesis. They monitored division time and abscission success in cells lacking Rab14. Fluorescence imaging was used to track Rab11-endosome localization at the intracellular bridge. Actin clearance at the abscission site was measured using live-cell imaging. The team tested whether Rab14 knockout affects microtubule dynamics during division. They performed binding assays to determine if Rab14 interacts with the MACF2/CAMSAP3 complex. The researchers used immunoprecipitation to confirm the physical interaction between Rab14 and MACF2. These methods allowed them to assess the functional role of Rab14 in endosome targeting.

Main Results:

Depletion of Rab14 caused cytokinesis failure or significantly prolonged division time. Rab14 knockout reduced the efficiency of Rab11-endosome recruitment to the intracellular bridge. The absence of Rab14 inhibited actin clearance at the abscission site. Rab14 was shown to bind to the MACF2/CAMSAP3 complex, which interacts with microtubule minus ends. This binding affected the targeting of endosomes to the intracellular bridge microtubules. Rab14 depletion disrupted the coordination of actin and microtubule dynamics during abscission. The study found no evidence that Rab14 regulates microtubule polymerization directly. Collectively, these findings suggest Rab14 regulates endosome targeting and actin clearance.

Conclusions:

The data suggest that Rab14 regulates endosome targeting during cytokinesis. Rab14 may contribute to the efficiency of Rab11-endosome recruitment to the intracellular bridge. The absence of Rab14 inhibits actin clearance at the abscission site. Rab14 appears to bind to the MACF2/CAMSAP3 complex, which influences endosome localization. This interaction may affect how endosomes are targeted to the intracellular bridge. The findings indicate that Rab14 and MACF2/CAMSAP3 regulate actin depolymerization. The study did not establish whether Rab14 is essential for microtubule dynamics. The results suggest a new regulatory mechanism for cytokinesis.

The study shows that Rab14 regulates endosome targeting and actin clearance during cytokinesis.

Researchers used depletion experiments to assess the effects on division time and abscission.

The MACF2/CAMSAP3 complex interacts with microtubule minus ends and influences endosome targeting.

Rab14 knockout inhibits actin clearance at the abscission site, suggesting a regulatory role.

Fluorescence imaging tracked Rab11-endosome recruitment to the intracellular bridge.

The findings suggest Rab14 and MACF2/CAMSAP3 regulate actin depolymerization during division.