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Specific role for the PH domain of dynamin‐1 in the regulation of rapid endocytosis in adrenal chromaffin cells
Author(s) -
Artalejo Cristina R.,
Lemmon Mark A.,
Schlessinger Joseph,
Palfrey H.Clive
Publication year - 1997
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/16.7.1565
Subject(s) - dynamin , biology , endocytosis , microbiology and biotechnology , chromaffin cell , receptor mediated endocytosis , endocrinology , receptor , biochemistry , adrenal medulla , catecholamine
Dynamin plays a key role in the scission event common to various types of endocytosis. We demonstrate that the pleckstrin homology (PH) domain of dynamin‐1 is critical in the process of rapid endocytosis (RE) in chromaffin cells. Introduction of this isolated PH domain into cells at concentrations as low as 1 μM completely suppressed RE. PH domains from other proteins, including that from the closely related dynamin‐2, were ineffective as inhibitors, even at high concentrations. Mutational studies indicated that a pair of isoform‐specific amino acids, located in a variable loop between the first two β‐strands, accounted for the differential effect of the two dynamin PH domains. Switching these amino acids in the dynamin‐2 PH domain to the equivalent residues in dynamin‐1 (SL→GI) generated a molecule that blocked RE. Thus, the PH domain of dynamin‐1 is essential for RE and exhibits a precise molecular selectivity. As chromaffin cells express both dynamin‐1 and ‐2, we speculate that different isoforms of dynamin may regulate distinct endocytotic processes and that the PH domain contributes to this specificity.