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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
22
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pubmed:dateCreated |
1998-1-5
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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.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/9362482-1281477,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9362482-1311055,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9362482-1421574,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9362482-1898771,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9362482-2099381,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9362482-334247,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9362482-7505438,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9362482-7537212,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9362482-7539429,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9362482-7539430,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9362482-7592898,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9362482-7667278,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9362482-7877694,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9362482-7962076,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9362482-8101525,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9362482-8266082,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9362482-8325879,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9362482-8349610,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9362482-8529632,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9362482-8568861,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9362482-8593162,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9362482-8666662,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9362482-8798389,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9362482-8910402,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9362482-8939066,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9362482-8947047,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9362482-9012790
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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 |
0261-4189
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
17
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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 |
6676-83
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:9362482-Dynamins,
pubmed-meshheading:9362482-Enzyme Activation,
pubmed-meshheading:9362482-GTP Phosphohydrolases,
pubmed-meshheading:9362482-Guanosine Triphosphate,
pubmed-meshheading:9362482-Hydrolysis,
pubmed-meshheading:9362482-Models, Molecular,
pubmed-meshheading:9362482-Peptide Fragments,
pubmed-meshheading:9362482-Protein Conformation,
pubmed-meshheading:9362482-Recombinant Proteins,
pubmed-meshheading:9362482-Sequence Analysis
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pubmed:year |
1997
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pubmed:articleTitle |
Domain structure and intramolecular regulation of dynamin GTPase.
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pubmed:affiliation |
Department of Cell Biology, The Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla, CA 92037, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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