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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
40
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pubmed:dateCreated |
2000-11-1
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pubmed:abstractText |
Dynamin is a large GTPase involved in the regulation of membrane constriction and fission during receptor-mediated endocytosis. Dynamin contains a pleckstrin-homology domain which is essential for endocytosis and which binds to anionic phospholipids. Here, we show for the first time that dynamin is a membrane-active molecule capable of penetrating into the acyl chain region of membrane lipids. Lipid penetration is strongly stimulated by phosphatidic acid (PA), phosphatidylinositol 4-phosphate, and phosphatidylinositol 4, 5-bisphosphate. Though binding is more efficient in the presence of the phosphoinositides, a much larger part of the dynamin molecule penetrates into PA-containing mixed-lipid systems. Thus, local lipid metabolism will dramatically influence dynamin-lipid interactions, and dynamin-lipid interactions are likely to play an important role in dynamin-dependent endocytosis. Our data suggest that dynamin is directly involved in membrane destabilization, a prerequisite to membrane fission.
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pubmed:grant |
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/1,2-dioleoylphosphatidylserine,
http://linkedlifedata.com/resource/pubmed/chemical/Blood Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Dynamins,
http://linkedlifedata.com/resource/pubmed/chemical/GTP Phosphohydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Lipids,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositols,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylserines,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/platelet protein P47
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0006-2960
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
39
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
12485-93
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:11015230-Animals,
pubmed-meshheading:11015230-Binding Sites,
pubmed-meshheading:11015230-Blood Platelets,
pubmed-meshheading:11015230-Blood Proteins,
pubmed-meshheading:11015230-Cattle,
pubmed-meshheading:11015230-Dynamins,
pubmed-meshheading:11015230-Endocytosis,
pubmed-meshheading:11015230-GTP Phosphohydrolases,
pubmed-meshheading:11015230-Genetic Vectors,
pubmed-meshheading:11015230-Humans,
pubmed-meshheading:11015230-Intracellular Membranes,
pubmed-meshheading:11015230-Membrane Lipids,
pubmed-meshheading:11015230-Microtubules,
pubmed-meshheading:11015230-Phosphatidic Acids,
pubmed-meshheading:11015230-Phosphatidylinositols,
pubmed-meshheading:11015230-Phosphatidylserines,
pubmed-meshheading:11015230-Phosphoproteins,
pubmed-meshheading:11015230-Protein Structure, Tertiary,
pubmed-meshheading:11015230-Recombinant Proteins,
pubmed-meshheading:11015230-Sequence Homology, Amino Acid,
pubmed-meshheading:11015230-Spodoptera
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pubmed:year |
2000
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pubmed:articleTitle |
Dynamin is membrane-active: lipid insertion is induced by phosphoinositides and phosphatidic acid.
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pubmed:affiliation |
Department of Biochemistry of Membranes, Centre for Biomembranes and Lipid Enzymology, Institute of Biomembranes, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands. K.N.J.Burger@bio.uu.nl
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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