Alternate pleckstrin homology domain orientations regulate dynamin-catalyzed membrane fission.

ABSTRACT: The self-assembling GTPase dynamin catalyzes endocytic vesicle scission via membrane insertion of its pleckstrin homology (PH) domain. However, the molecular mechanisms underlying PH domain-dependent membrane fission remain obscure. Membrane-curvature-sensing and membrane-curvature-generating properties have been attributed, but it remains to be seen whether the PH domain is involved in either process independent of dynamin self-assembly. Here, using multiple fluorescence spectroscopic and microscopic techniques, we demonstrate that the isolated PH domain does not act to bend membranes but instead senses high membrane curvature through hydrophobic insertion into the membrane bilayer. Furthermore, we use a complementary set of short- and long-distance Förster resonance energy transfer appro

SUBMITTER: Mehrotra N 

PROVIDER: S-EPMC3952856 | biostudies-literature | 2014 Mar

REPOSITORIES: biostudies-literature