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PMID: 1532721 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Review

Motor proteins for cytoplasmic microtubules.

Current opinion in cell biology ·Vol. 4 ·No. 1 ·1992-02-00 ·Pages 66-73

Bloom GS

Abstract

It has been thought that motile structures within the cell are driven toward the plus and minus ends of microtubules by the ATPases, kinesin and dynein, respectively. Recently obtained data indicate that this model is far too simplistic. Kinesin is now understood to be one representative of a family of proteins. Another member of the kinesin family has been found to generate force toward the microtubule minus end. Evidence for either a bidirectional dynein, or closely related retrograde and anterograde forms of dynein has also received potent new support. The discovery of a third potential microtubule motor, the GTPase, 'dynamin', complicates matters further.

MeSH Terms
Animals Ca(2+) Mg(2+)-ATPase/physiology Cell Cycle/physiology Cytoplasm/physiology Dynamins Dyneins/physiology Kinesins/physiology Microtubules/physiology Mitosis/physiology Structure-Activity Relationship
Chemicals
Ca(2+) Mg(2+)-ATPase Dyneins Kinesins Dynamins
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Bloom G S
Department of Cell Biology and Neuroscience, University of Texas Southwestern Medical Center, Dallas 75235.
Article Info
Journal
Current opinion in cell biology
Abbr.
Curr Opin Cell Biol
ISSN
0955-0674
Published
1992-02-00
Pages
66-73
Language
English
Region
England
NLM ID
8913428
Subset
IM
Grants
NINDS NIH HHS · NS23868 · United States
Corrections
ErratumIn
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