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Related Concept Videos

Microtubules01:35

Microtubules

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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.
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Microtubules01:18

Microtubules

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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....
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Microtubule Associated Proteins (MAPs)01:42

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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 Associated Motor Proteins01:32

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Eukaryotic cells have different motor proteins for transporting various cargo within the cell. These motor proteins differ based on the filament they associate with, the direction they move within the cell, and the type of cargo they transport. Motor proteins that associate with microtubules are known as microtubule-associated motor proteins. There are two families of microtubule-associated motor proteins —Kinesins and Dyneins. Both these proteins assist in the transport of cellular...
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Microtubule Instability02:17

Microtubule Instability

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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...
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Microtubule Formation01:23

Microtubule Formation

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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...
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Extracting Modified Microtubules from Mammalian Cells to Study Microtubule-Protein Complexes by Cryo-Electron Microscopy
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Platelet Microtubule Subunit Proteins.

A G Castle1, N Crawford1

  • 1The Department of Biochemistry, University of Birmingham, Birmingham, U. K.

Thrombosis and Haemostasis
|February 21, 2019
PubMed
Summary
This summary is machine-generated.

Blood platelets contain microtubule proteins, including tubulin and high molecular weight proteins (HMWs), that can polymerize in vitro. These platelet microtubules share characteristics with neurotubulins and are essential for cell structure.

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Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
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Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • Blood platelets contain microtubule proteins, specifically tubulin and high molecular weight proteins (HMWs).
  • These proteins can polymerize in vitro into structures resembling intact platelet microtubules.

Purpose of the Study:

  • To characterize the microtubule proteins found in blood platelets.
  • To investigate the properties and assembly of platelet microtubules.

Main Methods:

  • In vitro polymerization of platelet microtubule proteins.
  • Alkaline SDS-polyacrylamide gel electrophoresis to resolve tubulin subunits.
  • Sedimentation analysis to determine dimer characteristics.
  • Colchicine binding assays.
  • Immunofluorescence staining using antibodies against platelet and brain tubulins.

Main Results:

  • Platelet tubulin consists of two non-identical subunits (alpha and beta tubulin), each with a molecular weight of approximately 55,000 Daltons.
  • Tubulin subunits associate as dimers (5.7 S) that bind colchicine with kinetics similar to neurotubulins.
  • Platelet microtubules contain two essential HMW proteins (>200,000 Daltons).
  • Antibodies to tubulin stained filamentous structures in epithelial cells, which depolymerized under specific conditions.

Conclusions:

  • Platelet microtubules are composed of tubulin dimers and essential HMW proteins.
  • Platelet tubulin shares functional similarities with neurotubulin.
  • These findings contribute to understanding microtubule dynamics and composition in non-neuronal cells.