Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Binding Sites
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Blood Platelets / chemistry
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Blood Proteins / chemistry
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Cattle
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Dynamins
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Endocytosis
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GTP Phosphohydrolases / chemistry*
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GTP Phosphohydrolases / genetics
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GTP Phosphohydrolases / metabolism*
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Genetic Vectors
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Humans
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Intracellular Membranes / chemistry
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Intracellular Membranes / metabolism*
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Membrane Lipids / chemistry
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Membrane Lipids / metabolism*
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Microtubules / chemistry
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Microtubules / metabolism
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Phosphatidic Acids / chemistry*
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Phosphatidylinositols / chemistry*
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Phosphatidylserines / chemistry
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Phosphoproteins / chemistry
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Protein Structure, Tertiary / genetics
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
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Sequence Homology, Amino Acid
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Spodoptera / genetics
Substances
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Blood Proteins
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Membrane Lipids
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Phosphatidic Acids
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Phosphatidylinositols
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Phosphatidylserines
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Phosphoproteins
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Recombinant Proteins
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platelet protein P47
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1,2-dioleoylphosphatidylserine
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GTP Phosphohydrolases
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Dynamins