Abstract
We previously identified two forms of endocytosis using capacitance measurements in chromaffin cells: rapid endocytosis (RE), dynamin-1 dependent but clathrin-independent and slow endocytosis (SE), dynamin-2 and clathrin-dependent. Various recombinant SH3 domains that interact with the proline-rich domain of dynamin were introduced into single cells via the patch pipette. GST-SH3 domains of amphiphysin-1, intersectin-IC, and endophilin-I inhibited SE but had no effect on RE. Grb2-SH3 (N-terminal) or a mutant of amphiphysin-1-SH3 was inactive on either process. These data confirm that dynamin-1 dependent RE is independent of clathrin and show that amphiphysin is exclusively associated with clathrin and dynamin-2-dependent SE.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Acyltransferases / genetics
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Acyltransferases / metabolism
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Adaptor Proteins, Vesicular Transport / genetics
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Adaptor Proteins, Vesicular Transport / metabolism
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Adrenal Glands / cytology*
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Adrenal Glands / physiology
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Animals
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Antibodies / pharmacology
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Cattle
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Chromaffin Cells / drug effects
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Chromaffin Cells / metabolism
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Chromaffin Cells / physiology*
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Clathrin / metabolism
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Dynamin I / metabolism
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Dynamin II / metabolism
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Electric Capacitance
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Endocytosis / drug effects
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Endocytosis / physiology*
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Nerve Tissue Proteins / antagonists & inhibitors
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Nerve Tissue Proteins / genetics
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Nerve Tissue Proteins / metabolism*
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Recombinant Proteins / pharmacology
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Surface Plasmon Resonance
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src Homology Domains / genetics
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src Homology Domains / physiology*
Substances
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Adaptor Proteins, Vesicular Transport
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Antibodies
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Clathrin
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Nerve Tissue Proteins
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Recombinant Proteins
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intersectin 1
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amphiphysin
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Acyltransferases
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2-acylglycerophosphate acyltransferase
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Dynamin I
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Dynamin II