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Related Concept Videos

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...
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...
Anaphase A and B01:39

Anaphase A and B

Microtubules form through the end-to-end polymerization of tubulin heterodimers. Kinetochore microtubules originate from the spindle poles, and their plus-ends connect with the kinetochores on sister-chromatids. Ndc80 protein complexes, present on the kinetochore, form low-affinity links with the plus end of these kinetochore microtubules.
Plus-end depolymerization releases tubulin heterodimers from the terminal region of the microtubule. As tubulin subunits are lost, the Ndc80 complexes detach...
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...

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Using plusTipTracker Software to Measure Microtubule Dynamics in Xenopus laevis Growth Cones
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Microtubule tip-interacting proteins: a view from both ends.

Kai Jiang1, Anna Akhmanova

  • 1Department of Cell Biology, Erasmus Medical Center, P.O. Box 2040, 3000 CA Rotterdam, The Netherlands.

Current Opinion in Cell Biology
|September 7, 2010
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Summary

Microtubule ends are key for tubulin dynamics and cellular structure attachment. Diverse proteins bind these ends, regulating microtubule function and interactions.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Microtubule ends are dynamic sites for tubulin addition/removal.
  • Plus and minus ends have distinct properties and regulatory factors.
  • Proteins like gamma-tubulin, kinesins, and EB1 associate with microtubule tips.

Purpose of the Study:

  • To overview microtubule tip-interacting proteins.
  • To explain mechanisms of protein association with microtubule ends.
  • To discuss functional crosstalk between plus and minus-end binding factors.

Main Methods:

  • Literature review of microtubule dynamics and associated proteins.
  • Analysis of protein-microtubule end interaction mechanisms.
  • Synthesis of functional crosstalk between different tip-binding factors.

Main Results:

  • Microtubule ends are regulated by specific capping factors, motors, and plus-end tracking proteins.
  • Diverse mechanisms mediate the association of these proteins with microtubule tips.
  • Functional interactions exist between proteins binding to opposite microtubule ends.

Conclusions:

  • Microtubule ends are critical hubs for cellular organization and dynamics.
  • A complex network of proteins regulates microtubule behavior at its tips.
  • Understanding these interactions provides insights into microtubule-based cellular processes.