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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
11
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pubmed:dateCreated |
2005-10-28
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pubmed:abstractText |
CLIP-170 belongs to a group of proteins (+TIPs) with the enigmatic ability to dynamically track growing microtubule plus-ends. CLIP-170 regulates microtubule dynamics in vivo and has been implicated in cargo-microtubule interactions in vivo and in vitro. Though plus-end tracking likely has intimate connections to +TIP function, little is known about the mechanism(s) by which this dynamic localization is achieved. Using a combination of biochemistry and live cell imaging, we provide evidence that CLIP-170 tracks microtubule plus-ends by a preassociation, copolymerization, and regulated release mechanism. As part of this analysis, we find that CLIP-170 has a stronger affinity for tubulin dimer than for polymer, and that CLIP-170 can distinguish between GTP- and GDP-like polymer. This work extends the previous analysis of CLIP-170 behavior in vivo and complements the existing fluorescence microscope characterization of CLIP-170 interactions with microtubules in vitro. In particular, these data explain observations that CLIP-170 localizes to newly polymerized microtubules in vitro but cannot track microtubule plus-ends in vitro. These observations have implications for the functions of CLIP-170 in regulating microtubule dynamics.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16120651-10030671,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16120651-10052454,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/16120651-9885247
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
1059-1524
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
16
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5373-84
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:16120651-Animals,
pubmed-meshheading:16120651-Fluorescence Polarization,
pubmed-meshheading:16120651-GTP-Binding Proteins,
pubmed-meshheading:16120651-HeLa Cells,
pubmed-meshheading:16120651-Humans,
pubmed-meshheading:16120651-Kymography,
pubmed-meshheading:16120651-Microtubule-Associated Proteins,
pubmed-meshheading:16120651-Microtubules,
pubmed-meshheading:16120651-Models, Biological,
pubmed-meshheading:16120651-Neoplasm Proteins,
pubmed-meshheading:16120651-Tubulin
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pubmed:year |
2005
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pubmed:articleTitle |
Interactions between CLIP-170, tubulin, and microtubules: implications for the mechanism of Clip-170 plus-end tracking behavior.
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pubmed:affiliation |
Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN 46565, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
In Vitro,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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