Two mechanistically distinct forms of endocytosis in adrenal chromaffin cells: Differential effects of SH3 domains and amphiphysin antagonism.
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.
Mesh Terms:
Acyltransferases, Adaptor Proteins, Vesicular Transport, Adrenal Glands, Animals, Antibodies, Cattle, Chromaffin Cells, Clathrin, Dynamin I, Dynamin II, Electric Capacitance, Endocytosis, Nerve Tissue Proteins, Recombinant Proteins, Surface Plasmon Resonance, src Homology Domains
Acyltransferases, Adaptor Proteins, Vesicular Transport, Adrenal Glands, Animals, Antibodies, Cattle, Chromaffin Cells, Clathrin, Dynamin I, Dynamin II, Electric Capacitance, Endocytosis, Nerve Tissue Proteins, Recombinant Proteins, Surface Plasmon Resonance, src Homology Domains
FEBS Lett.
Date: May. 29, 2006
PubMed ID: 16696976
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