Document Detail


Katanin, the microtubule-severing ATPase, is concentrated at centrosomes.
MedLine Citation:
PMID:  8907702     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The assembly and function of the mitotic spindle involve specific changes in the dynamic properties of microtubules. One such change results in the poleward flux of tubulin in which spindle microtubules polymerize at their kinetochore-attached plus ends while they shorten at their centrosome-attached minus ends. Since free microtubule minus ends do not depolymerize in vivo, the poleward flux of tubulin suggests that spindle microtubules are actively disassembled at or near their centrosomal attachment points. The microtubule-severing ATPase, katanin, has the ability actively to sever and disassemble microtubules and is thus a candidate for the role of a protein mediating the poleward flux of tubulin. Here we determine the subcellular localization of katanin by immunofluorescence as a preliminary step in determining whether katanin mediates the poleward flux of tubulin. We find that katanin is highly concentrated at centrosomes throughout the cell cycle. Katanin's localization is different from that of gamma-tubulin in that microtubules are required to maintain the centrosomal localization of katanin. Direct comparison of the localization of katanin and gamma-tubulin reveals that katanin is localized in a region surrounding the gamma-tubulin-containing pericentriolar region in detergent-extracted mitotic spindles. The centrosomal localization of katanin is consistent with the hypothesis that katanin mediates the disassembly of microtubule minus ends during poleward flux.
Authors:
F J McNally; K Okawa; A Iwamatsu; R D Vale
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Journal of cell science     Volume:  109 ( Pt 3)     ISSN:  0021-9533     ISO Abbreviation:  J. Cell. Sci.     Publication Date:  1996 Mar 
Date Detail:
Created Date:  1997-03-11     Completed Date:  1997-03-11     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0052457     Medline TA:  J Cell Sci     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  561-7     Citation Subset:  IM    
Affiliation:
Section of Molecular and Cellular Biology, University of California at Davis 95616, USA.
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MeSH Terms
Descriptor/Qualifier:
Adenosine Triphosphatases / analysis*
Amino Acid Sequence
Animals
Antibody Specificity
Cell Cycle / physiology
Centrosome / enzymology*
Microtubules / metabolism*
Molecular Sequence Data
Sea Urchins
Tubulin / analysis
Chemical
Reg. No./Substance:
0/Tubulin; EC 3.6.1.-/Adenosine Triphosphatases; EC 3.6.1.-/katanin

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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