Two mechanistically distinct forms of endocytosis in adrenal chromaffin cells: Differential effects of SH3 domains and amphiphysin antagonism |
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| Authors: | Elhamdani Abdeladim Azizi Fouad Solomaha Elena Palfrey H Clive Artalejo Cristina R |
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| Institution: | Department of Pharmacology, Wayne State University School of Medicine, Detroit, MI 48201, USA. aelhamda@med.wayne.edu |
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| 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. |
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| Keywords: | AC cells adrenal chromaffin cells APs action potentials RE rapid endocytosis SE slow endocytosis CCV clathrin-coated vesicle |
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