| Regulation of microtubule dynamic instability. | |
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MedLine Citation:
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PMID: 8299143 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Characterization of microtubule assembly in vivo and in vitro has raised questions of how cells regulate dynamic instability. While dynamic instability is an intrinsic property of the tubulin molecule, factors are required to increase the plus-end elongation rate and increase the frequencies of both catastrophe and rescue to achieve cellular tubulin turnover rates. It is likely that the activities of the transition frequency regulators are themselves regulated during the cell cycle, but the mechanisms of regulation are not known. As we identify the proteins which alter microtubule assembly, new classes of MAPs will emerge. An understanding of how these proteins function may provide further insight into how cells organize the different arrays of microtubules used for such processes as vesicle transport, polarized organization of organelles, and chromosome movement. |
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Authors:
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L Cassimeris |
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Publication Detail:
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Type: Journal Article; Review |
Journal Detail:
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Title: Cell motility and the cytoskeleton Volume: 26 ISSN: 0886-1544 ISO Abbreviation: Cell Motil. Cytoskeleton Publication Date: 1993 |
Date Detail:
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Created Date: 1994-03-10 Completed Date: 1994-03-10 Revised Date: 2005-11-16 |
Medline Journal Info:
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Nlm Unique ID: 8605339 Medline TA: Cell Motil Cytoskeleton Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 275-81 Citation Subset: IM |
Affiliation:
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Department of Molecular Biology, Lehigh University, Bethlehem, Pennsylvania 18015. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Cell Cycle / physiology Cell Polarity / physiology Microtubule-Associated Proteins / physiology Microtubules / physiology* Tubulin / chemistry, metabolism |
| Chemical | |
Reg. No./Substance:
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0/Microtubule-Associated Proteins; 0/Tubulin |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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