Document Detail

Microtubule depolymerization at high pressure.
MedLine Citation:
PMID:  20233372     Owner:  NLM     Status:  MEDLINE    
We performed in vitro assays to visualize the effects of pressure on the filamentous structure of microtubules. Taxol-stabilized microtubules were tethered to kinesin motors on the observation window of a high-pressure chamber. When pressure was applied to the sample solution, all of the microtubules started to shorten from both ends. The length changes were constant over time, irrespective of the microtubule polarity. The shortening rate of microtubules increased exponentially with pressure, and the activation volume was -100 mL/mol, consistent with in vivo studies. These results show that application of pressure works directly to weaken the intermolecular interactions between tubulin molecules.
Masayoshi Nishiyama; Yoshiki Shimoda; Manabu Hasumi; Yoshifumi Kimura; Masahide Terazima
Publication Detail:
Type:  In Vitro; Journal Article    
Journal Detail:
Title:  Annals of the New York Academy of Sciences     Volume:  1189     ISSN:  1749-6632     ISO Abbreviation:  Ann. N. Y. Acad. Sci.     Publication Date:  2010 Feb 
Date Detail:
Created Date:  2010-03-17     Completed Date:  2010-04-02     Revised Date:  2010-10-19    
Medline Journal Info:
Nlm Unique ID:  7506858     Medline TA:  Ann N Y Acad Sci     Country:  United States    
Other Details:
Languages:  eng     Pagination:  86-90     Citation Subset:  IM    
Department of Chemistry, Kyoto University, Japan.
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MeSH Terms
Biotechnology / instrumentation
Cytoskeleton / chemistry
Hydrostatic Pressure*
Kinesin / chemistry
Microscopy, Fluorescence / instrumentation
Microtubules / chemistry*,  ultrastructure*
Molecular Motor Proteins / chemistry
Polymers / chemistry
Tubulin / chemistry
Water / chemistry
Reg. No./Substance:
0/Molecular Motor Proteins; 0/Polymers; 0/Tubulin; 7732-18-5/Water; EC 3.6.1.-/Kinesin

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