Ontology highlight
ABSTRACT:
SUBMITTER: Holkar SS
PROVIDER: S-EPMC4505496 | biostudies-literature | 2015 Jun
REPOSITORIES: biostudies-literature
Holkar Sachin S SS Kamerkar Sukrut C SC Pucadyil Thomas J TJ
The Journal of biological chemistry 20150402 23
Epsins belong to the family of highly conserved clathrin-associated sorting proteins that are indispensable for clathrin-mediated endocytosis, but their precise functions remain unclear. We have developed an assay system of budded supported membrane tubes displaying planar and highly curved membrane surfaces to analyze intrinsic membrane curvature preference shown by clathrin-associated sorting proteins. Using real-time fluorescence microscopy, we find that epsin preferentially partitions to and ...[more]