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Overview of Secretory Vesicles01:33

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Secretory vesicles, also known as dense core vesicles (DCVs), are membrane-bound vesicles that transport secretory proteins, such as hormones or neurotransmitters. Regulated secretory vesicles transport proteins from the trans-Golgi network to the exterior of the cell. Proteins present in regulated secretory vesicles are required to be rapidly exocytosed in large amounts upon a specific stimulus.
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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.
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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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Cell polarity is the asymmetric distribution of cellular and membrane components, making one side of the cell different from the other. This polarity is essential to many processes such as embryogenesis, axon migration, glucose transport across epithelial cells, and directional cell migration. A migrating cell responds to intracellular or extracellular signals via molecular cascades that reorganize the actin cytoskeleton to establish this polarity. In these cells, the Rho family proteins Cdc42,...
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  5. Cellular Interactions (incl. Adhesion, Matrix, Cell Wall)
  6. Spatial Control Of Secretory Vesicle Targeting By The Ync13-rga7-rng10 Complex During Cytokinesis

Spatial control of secretory vesicle targeting by the Ync13-Rga7-Rng10 complex during cytokinesis

Sha Zhang1, Davinder Singh1, Yi-Hua Zhu1

  • 1Department of Molecular Genetics, The Ohio State University, Columbus, OH 43210, USA.

Biorxiv : the Preprint Server for Biology
|June 4, 2025

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Spatiotemporal Analysis of Cytokinetic Events in Fission Yeast
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View abstract on PubMed

Summary
This summary is machine-generated.

A conserved protein module precisely targets vesicles during cell division, ensuring proper septum formation and cell integrity. This discovery sheds light on membrane trafficking control in cytokinesis.

Area of Science:

  • Cell biology
  • Molecular and cell biology
  • Biochemistry

Background:

  • Cytokinesis, or cell division, requires coordinated membrane trafficking for cell integrity.
  • Mechanisms controlling vesicle targeting during cytokinesis remain incompletely understood.
  • Key proteins involved in cytokinesis are conserved across eukaryotes.

Purpose of the Study:

  • To identify molecular mechanisms regulating vesicle targeting during fission yeast cytokinesis.
  • To elucidate the roles of specific proteins in membrane trafficking at the cleavage furrow.

Main Methods:

  • Fission yeast genetics
  • Fluorescence microscopy
  • In vitro binding assays

Main Results:

Keywords:
Ags1Bgs4Sec1Smi1

Related Experiment Videos

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  • Identified a conserved module (Ync13, Rga7, Rng10) critical for vesicle targeting during cytokinesis.
  • This module recruits the TRAPP-II complex to deliver glucan synthases (Bgs4, Ags1) to the cleavage furrow.
  • Ync13 interacts with Sec1 for vesicle fusion, and mutations disrupt septum integrity, causing cell lysis.

Conclusions:

  • The Ync13-Rga7-Rng10 module ensures precise vesicle targeting and fusion during cytokinesis.
  • This pathway is essential for maintaining cell integrity by proper septum formation.
  • Provides novel insights into the spatiotemporal regulation of membrane trafficking in cell division.
TRAPP-II complex
cytokinesis
fission yeast
septum