Ontology highlight
ABSTRACT:
SUBMITTER: Dar S
PROVIDER: S-EPMC5221619 | biostudies-literature | 2017 Jan
REPOSITORIES: biostudies-literature
Dar Srishti S Pucadyil Thomas J TJ
Molecular biology of the cell 20161109 1
Classical dynamins bind the plasma membrane-localized phosphatidylinositol-4,5-bisphosphate using the pleckstrin-homology domain (PHD) and engage in rapid membrane fission during synaptic vesicle recycling. This domain is conspicuously absent among extant bacterial and mitochondrial dynamins, however, where loop regions manage membrane recruitment. Inspired by the core design of bacterial and mitochondrial dynamins, we reengineered the classical dynamin by replacing its PHD with a polyhistidine ...[more]