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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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Controlling Flow Speeds of Microtubule-Based 3D Active Fluids Using Temperature
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Published on: November 26, 2019

MAP6-F is a temperature sensor that directly binds to and protects microtubules from cold-induced depolymerization.

Christian Delphin1, Denis Bouvier2, Maxime Seggio1

  • 1Team 1 Physiopathology of Cytoskeleton; Commissariat à I'Energie Atomique, Institut National de la Santé et de la Recherche Médicale, U836-GIN iRTSV-GPC, Site Santé La Tronche, BP170, 38042 Grenoble, Cedex 9, France.

The Journal of Biological Chemistry
|August 21, 2012
PubMed
Summary

Microtubule-associated protein 6 (MAP6) stabilizes cellular microtubules at low temperatures. This protein acts as a temperature sensor, adapting its conformation to maintain microtubule integrity in organisms experiencing cold.

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Area of Science:

  • Cell Biology
  • Biochemistry
  • Structural Biology

Background:

  • Microtubules are essential cellular structures known to be unstable at cold temperatures in vitro.
  • Microtubule-associated protein 6 (MAP6) protects microtubules from cold-induced depolymerization in vivo.
  • The precise mechanism of MAP6-mediated microtubule stabilization at low temperatures and the extent of cold sensitivity across physiological temperature ranges remain unclear.

Purpose of the Study:

  • To investigate the mechanism by which MAP6 stabilizes microtubules at 4 °C.
  • To determine the temperature-dependent sensitivity of microtubules in vivo.
  • To elucidate the role of MAP6 as a potential temperature sensor.

Main Methods:

  • Cellular experiments observing microtubule depolymerization at temperatures below 20 °C in the presence and absence of MAP6.
  • Analysis of MAP6-F binding dynamics and microtubule stabilization within cells.
  • Biochemical assays using purified proteins to study MAP6-F binding to microtubules.
  • Circular dichroism spectroscopy to detect conformational changes in the MAP6-F Mc domain.

Main Results:

  • In the absence of MAP6, cellular microtubules depolymerize rapidly and in a temperature-dependent manner below 20 °C.
  • MAP6 presence stabilizes microtubules against cold-induced depolymerization.
  • MAP6-F binding to microtubules is dynamic and temperature-dependent, suggesting temperature directly influences complex formation.
  • Purified MAP6-F directly binds microtubules via its Mc domain in a temperature-dependent manner, accompanied by conformational changes.

Conclusions:

  • MAP6 is crucial for maintaining microtubule stability at reduced temperatures.
  • MAP6 functions as a temperature sensor, altering its conformation to stabilize microtubules.
  • This temperature-sensing mechanism is vital for preserving the microtubule network in organisms exposed to decreasing temperatures, such as during hibernation.