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J Cell Biol. 2014 Nov 10;207(3):323-34. doi: 10.1083/jcb.201407095.

The contribution of αβ-tubulin curvature to microtubule dynamics.

Author information

1
Department of Biology, McGill University, Montréal, Quebec, Canada H3A1B1 gary.brouhard@mcgill.ca luke.rice@utsouthwestern.edu.
2
Department of Biophysics and Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75390 Department of Biophysics and Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75390 gary.brouhard@mcgill.ca luke.rice@utsouthwestern.edu.

Abstract

Microtubules are dynamic polymers of αβ-tubulin that form diverse cellular structures, such as the mitotic spindle for cell division, the backbone of neurons, and axonemes. To control the architecture of microtubule networks, microtubule-associated proteins (MAPs) and motor proteins regulate microtubule growth, shrinkage, and the transitions between these states. Recent evidence shows that many MAPs exert their effects by selectively binding to distinct conformations of polymerized or unpolymerized αβ-tubulin. The ability of αβ-tubulin to adopt distinct conformations contributes to the intrinsic polymerization dynamics of microtubules. αβ-Tubulin conformation is a fundamental property that MAPs monitor and control to build proper microtubule networks.

PMID:
25385183
PMCID:
PMC4226729
DOI:
10.1083/jcb.201407095
[Indexed for MEDLINE]
Free PMC Article

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