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Related Concept Videos

Microtubule Instability02:17

Microtubule Instability

Microtubules are hollow cylindrical filaments having a diameter of approximately 25 nm and a length that varies from 200 nm to 25 μm. GTP-bound tubulin subunits form αβ-heterodimers for microtubule assembly. These core building blocks interact longitudinally, polymerizing into protofilaments. The protofilaments then interact with one another through lateral bonding forces to form stable cylindrical microtubules. These cylindrical filaments are dynamic as they undergo repeated assembly and...
Microtubule Instability02:17

Microtubule Instability

Microtubules are hollow cylindrical filaments having a diameter of approximately 25 nm and a length that varies from 200 nm to 25 μm. GTP-bound tubulin subunits form αβ-heterodimers for microtubule assembly. These core building blocks interact longitudinally, polymerizing into protofilaments. The protofilaments then interact with one another through lateral bonding forces to form stable cylindrical microtubules. These cylindrical filaments are dynamic as they undergo repeated assembly and...
Microtubule Formation01:23

Microtubule Formation

Microtubules are dynamic structures that undergo continuous assembly and disassembly. They originate from specialized multi-protein complexes known as microtubule organizing centers or MTOCs. Within the MTOC, the point of origin of the microtubule is known as the minus end, while the end radiating outward is the plus end. Microtubules serve two primary functions — the organization of spindle complexes to separate sister chromatids during mitotic or meiotic cell division and the formation of...
Microtubules01:18

Microtubules

Microtubules are the thickest cytoskeletal filaments with a diameter of 25 nm. In prokaryotic organisms, microtubules are commonly found in locomotory appendages like cilia and flagella. In eukaryotic cells, microtubules form specialized extensions for moving fluid over the surface, like those found in cells lining the intestine.
Microtubules have two structurally similar globular protein subunits: α and β tubulins. In the cytosol, the α and β tubulins form a heterodimer. These αβ-heterodimers...
Microtubules01:35

Microtubules

There are three types of cytoskeletal structures in eukaryotic cells—microfilaments, intermediate filaments, and microtubules. With a diameter of about 25 nm, microtubules are the thickest of these fibers. Microtubules carry out a variety of functions that include cell structure and support, transport of organelles, cell motility (movement), and the separation of chromosomes during cell division.Microtubules are hollow tubes whose walls are made up of globular tubulin proteins. Each tubulin...
Microtubule Associated Proteins (MAPs)01:42

Microtubule Associated Proteins (MAPs)

Microtubule function and architecture are regulated by an array of specialized proteins called microtubule-associated proteins or MAPs. These proteins are widespread across different organisms and have conserved protein motifs, like the multi-TOG domain for tubulin binding found in the CLASP family of MAPs. Some MAPs are lineage-specific based on their conserved domains. Their functions depend upon the cytoskeletal architecture and cell type they are located within. In-plant cells, a specific...

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Microtubule Plus-End Dynamics Visualization in Huntington's Disease Model based on Human Primary Skin Fibroblasts
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{gamma}-Tubulin ring complexes regulate microtubule plus end dynamics.

Anaïs Bouissou1, Christel Vérollet, Aureliana Sousa

  • 1Centre de Recherche en Pharmacologie-Santé, Unité Mixte de Recherche 2587 Centre National de la Recherche Scientifique-Pierre Fabre, 31400 Toulouse, France.

The Journal of Cell Biology
|December 2, 2009
PubMed
Summary
This summary is machine-generated.

The gamma-tubulin ring complex (gamma-TuRC) regulates microtubule dynamics during interphase. This complex, associated with microtubules, limits catastrophes and influences pause or rescue events.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Cytoskeleton Dynamics

Background:

  • Gamma-tubulin is essential for microtubule assembly.
  • In Drosophila, gamma-tubulin functions in gamma-tubulin small complexes (gamma-TuSC) and gamma-tubulin ring complexes (gamma-TuRC).
  • Gamma-TuRC components are vital for mitotic progression, but their interphase roles are unclear.

Purpose of the Study:

  • To investigate the role of the gamma-tubulin ring complex (gamma-TuRC) during interphase microtubule organization and dynamics.
  • To determine if gamma-TuRC components influence microtubule stability outside of mitosis.

Main Methods:

  • RNA interference (RNAi) in Drosophila S2 cells to deplete gamma-TuRC components.
  • Immunofluorescence microscopy to analyze microtubule organization.
  • Live imaging to observe microtubule dynamics in real-time.

Main Results:

  • Depletion of gamma-TuRC components did not disrupt overall microtubule organization.
  • Loss of gamma-TuRC components led to increased microtubule dynamics.
  • Gamma-TuRC was observed along interphase microtubules, with distal spots correlating with microtubule pause and rescue events.

Conclusions:

  • The gamma-tubulin ring complex (gamma-TuRC) regulates interphase microtubule dynamics, not just nucleation.
  • Gamma-TuRC associated with microtubules may limit catastrophe events, contributing to microtubule stability.
  • These findings reveal a novel role for gamma-TuRC in controlling microtubule behavior during interphase.