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C. Artalejo, John HENLEYt, Mark MCNIVENt, H. PALFREYt (1995)
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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.
The EMBO Journal – Wiley
Published: Jan 1, 1997
Keywords: ; ; ;
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