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PMID: 16230114 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Review

Microtubules and maps.

Advances in protein chemistry ·Vol. 71 ·2005-00-00 ·Pages 257-98

Amos LA, Schlieper D

Abstract

Microtubules are very dynamic polymers whose assembly and disassembly is determined by whether their heterodimeric tubulin subunits are in a straight or curved conformation. Curvature is introduced by bending at the interfaces between monomers. Assembly and disassembly are primarily controlled by the hydrolysis of guanosine triphosphate (GTP) in a site that is completed by the association of two heterodimers. However, a multitude of associated proteins are able to fine-tune these dynamics so that microtubules are assembled and disassembled where and when they are required by the cell. We review the recent progress that has been made in obtaining a glimpse of the structural interactions involved.

MeSH Terms
Animals Guanosine Triphosphate/chemistry,physiology Humans Microtubule-Associated Proteins/chemistry,pharmacology,physiology Microtubules/chemistry,drug effects,physiology Protein Conformation Protein Structure, Tertiary Tubulin/chemistry,drug effects,physiology
Chemicals
Microtubule-Associated Proteins Tubulin Guanosine Triphosphate
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Amos Linda A
MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, United Kingdom.
Schlieper Daniel
Article Info
Journal
Advances in protein chemistry
Abbr.
Adv Protein Chem
ISSN
0065-3233
Published
2005-00-00
Pages
257-98
Language
English
Region
United States
NLM ID
0116732
Subset
IM
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