| pubmed-article:9362482 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9362482 | lifeskim:mentions | umls-concept:C0058836 | lld:lifeskim |
| pubmed-article:9362482 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:9362482 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:9362482 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:9362482 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:9362482 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:9362482 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:9362482 | pubmed:issue | 22 | lld:pubmed |
| pubmed-article:9362482 | pubmed:dateCreated | 1998-1-5 | lld:pubmed |
| pubmed-article:9362482 | pubmed:abstractText | Dynamin is a 100 kDa GTPase required for receptor-mediated endocytosis, functioning as the key regulator of the late stages of clathrin-coated vesicle budding. It is specifically targeted to clathrin-coated pits where it self-assembles into 'collars' required for detachment of coated vesicles from the plasma membrane. Self-assembly stimulates dynamin GTPase activity. Thus, dynamin-dynamin interactions are critical in regulating its cellular function. We show by crosslinking and analytical ultracentrifugation that dynamin is a tetramer. Using limited proteolysis, we have defined structural domains of dynamin and evaluated the domain interactions and requirements for self-assembly and GTP binding and hydrolysis. We show that dynamin's C-terminal proline- and arginine-rich domain (PRD) and dynamin's pleckstrin homology (PH) domain are, respectively, positive and negative regulators of self-assembly and GTP hydrolysis. Importantly, we have discovered that the alpha-helical domain interposed between the PH domain and the PRD interacts with the N-terminal GTPase domain to stimulate GTP hydrolysis. We term this region the GTPase effector domain (GED) of dynamin. | lld:pubmed |
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| pubmed-article:9362482 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9362482 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9362482 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9362482 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9362482 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:9362482 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:9362482 | pubmed:author | pubmed-author:SchmidS LSL | lld:pubmed |
| pubmed-article:9362482 | pubmed:author | pubmed-author:WarnockD EDE | lld:pubmed |
| pubmed-article:9362482 | pubmed:author | pubmed-author:MuhlbergA BAB | lld:pubmed |
| pubmed-article:9362482 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9362482 | pubmed:day | 17 | lld:pubmed |
| pubmed-article:9362482 | pubmed:volume | 16 | lld:pubmed |
| pubmed-article:9362482 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9362482 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9362482 | pubmed:pagination | 6676-83 | lld:pubmed |
| pubmed-article:9362482 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:9362482 | pubmed:meshHeading | pubmed-meshheading:9362482-... | lld:pubmed |
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| pubmed-article:9362482 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9362482 | pubmed:articleTitle | Domain structure and intramolecular regulation of dynamin GTPase. | lld:pubmed |
| pubmed-article:9362482 | pubmed:affiliation | Department of Cell Biology, The Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla, CA 92037, USA. | lld:pubmed |
| pubmed-article:9362482 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9362482 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:9362482 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:9362482 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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