| pubmed-article:15175652 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15175652 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:15175652 | lifeskim:mentions | umls-concept:C0013352 | lld:lifeskim |
| pubmed-article:15175652 | lifeskim:mentions | umls-concept:C0085139 | lld:lifeskim |
| pubmed-article:15175652 | lifeskim:mentions | umls-concept:C0237876 | lld:lifeskim |
| pubmed-article:15175652 | lifeskim:mentions | umls-concept:C0185027 | lld:lifeskim |
| pubmed-article:15175652 | pubmed:issue | 13 | lld:pubmed |
| pubmed-article:15175652 | pubmed:dateCreated | 2004-7-7 | lld:pubmed |
| pubmed-article:15175652 | pubmed:abstractText | Dyneins and kinesins move in opposite directions on microtubules. The question of how the same-track microtubules are able to support movement in two directions remains unanswered due to the absence of details on dynein-microtubule interactions. To address this issue, we studied dynein-microtubule interactions using the tip of the microtubule-binding stalk, the dynein stalk head (DSH), which directly interacts with microtubules upon receiving conformational change from the ATPase domain. Biochemical and cryo-electron microscopic studies revealed that DSH bound to tubulin dimers with a periodicity of 80 A, corresponding to the step size of dyneins. The DSH molecule was observed as a globular corn grain-like shape that bound the same region as kinesin. Biochemical crosslinking experiments and image analyses of the DSH-kinesin head-microtubule complex revealed competition between DSH and the kinesin head for microtubule binding. Our results demonstrate that dynein and kinesin share an overlapping microtubule-binding site, and imply that binding at this site has an essential role for these motor proteins. | lld:pubmed |
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| pubmed-article:15175652 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15175652 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15175652 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15175652 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15175652 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:15175652 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:15175652 | pubmed:author | pubmed-author:HirokawaNobut... | lld:pubmed |
| pubmed-article:15175652 | pubmed:author | pubmed-author:ToyoshimaYoko... | lld:pubmed |
| pubmed-article:15175652 | pubmed:author | pubmed-author:EdamatsuMasak... | lld:pubmed |
| pubmed-article:15175652 | pubmed:author | pubmed-author:Watai-NishiiJ... | lld:pubmed |
| pubmed-article:15175652 | pubmed:author | pubmed-author:KikkawaMasahi... | lld:pubmed |
| pubmed-article:15175652 | pubmed:author | pubmed-author:TobaShioriS | lld:pubmed |
| pubmed-article:15175652 | pubmed:author | pubmed-author:MizunoNaokoN | lld:pubmed |
| pubmed-article:15175652 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15175652 | pubmed:day | 7 | lld:pubmed |
| pubmed-article:15175652 | pubmed:volume | 23 | lld:pubmed |
| pubmed-article:15175652 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15175652 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15175652 | pubmed:pagination | 2459-67 | lld:pubmed |
| pubmed-article:15175652 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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