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PMID: 11031231 Published · ppublish English Journal Article Review

Structural basis for the interaction of tubulin with proteins and drugs that affect microtubule dynamics.

Annual review of cell and developmental biology ·Vol. 16 ·2000-00-00 ·Pages 89-111

Downing KH

Abstract

The microtubule cytoskeleton is a highly regulated system. At different times in the cell cycle and positions within the organism, microtubules can be very stable or highly dynamic. Stability and dynamics are regulated by interaction with a large number of proteins that themselves may change at specific points in the cell cycle. Exogenous ligands can disrupt the normal processes by either increasing or decreasing microtubule stability and inhibiting their dynamic behavior. The recent determination of the structure of tubulin, the main component of microtubules, makes it possible now to begin to understand the details of these interactions. We review here the structure of the tubulin dimer, with particular regard to how proteins and drugs may bind and modulate microtubule dynamics.

MeSH Terms
Alkaloids/metabolism Animals Colchicine/metabolism Humans Microtubule-Associated Proteins/metabolism Microtubules/metabolism Paclitaxel/metabolism Protein Structure, Secondary Structure-Activity Relationship Tubulin/chemistry,metabolism Vinblastine/metabolism
Chemicals
Alkaloids Microtubule-Associated Proteins Tubulin Vinblastine Paclitaxel Colchicine
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Downing K H
Donner Laboratory, Life Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA. khdowning@lbl.gov
Article Info
Journal
Annual review of cell and developmental biology
Abbr.
Annu Rev Cell Dev Biol
ISSN
1081-0706
Published
2000-00-00
Pages
89-111
Language
English
Region
United States
NLM ID
9600627
Subset
IM
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