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Related Concept Videos

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...
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Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.
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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...
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Extracting Modified Microtubules from Mammalian Cells to Study Microtubule-Protein Complexes by Cryo-Electron Microscopy
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EBs recognize a nucleotide-dependent structural cap at growing microtubule ends.

Sebastian P Maurer1, Franck J Fourniol, Gergő Bohner

  • 1Cancer Research UK London Research Institute, Lincoln's Inn Fields Laboratories, 44 Lincoln's Inn Fields, London WC2A 3LY, UK.

Cell
|April 17, 2012
PubMed
Summary
This summary is machine-generated.

End-binding proteins (EBs) track growing microtubule ends by binding to specific structures. This study reveals how the Mal3 EB

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Area of Science:

  • Cell Biology
  • Structural Biology
  • Biochemistry

Background:

  • Growing microtubule ends are crucial binding sites for proteins regulating microtubule dynamics.
  • End-binding proteins (EBs) identify and bind to these dynamic microtubule ends, recruiting other factors.
  • The precise structural basis for EB recognition of growing microtubule ends remains largely unknown.

Purpose of the Study:

  • To determine the pseudoatomic model of how the calponin homology (CH) domain of fission yeast EB Mal3 binds to growing microtubule ends.
  • To elucidate the structural characteristics of the microtubule end region recognized by EBs.
  • To understand the relationship between microtubule end structure, EB binding, and microtubule dynamics.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) for high-resolution structural determination.
  • Subnanometer single-particle reconstruction to build the pseudoatomic model.
  • Fluorescence imaging to validate binding and dynamics in situ.

Main Results:

  • A pseudoatomic model of the Mal3 CH domain bound to growing microtubule ends was generated.
  • The Mal3 CH domain was observed to bridge microtubule protofilaments, excluding the seam.
  • Binding occurs near the GTP-binding site, suggesting sensitivity to nucleotide state.

Conclusions:

  • The structure reveals how EBs recognize and bind to dynamic microtubule ends.
  • EB binding is spatially linked to the microtubule's nucleotide-binding site, potentially sensing its state.
  • This provides a structural link between microtubule dynamic instability and the end-tracking mechanism of EBs.