Human Rab small GTPase- and class V myosin-mediated membrane tethering in a chemically defined reconstitution system.

ABSTRACT: Membrane tethering is a fundamental process essential for the compartmental specificity of intracellular membrane trafficking in eukaryotic cells. Rab-family small GTPases and specific sets of Rab-interacting effector proteins, including coiled-coil tethering proteins and multisubunit tethering complexes, are reported to be responsible for membrane tethering. However, whether and how these key components directly and specifically tether subcellular membranes remains enigmatic. Using chemically defined proteoliposomal systems reconstituted with purified human Rab proteins and synthetic liposomal membranes to study the molecular basis of membrane tethering, we established here that Rab-family GTPases have a highly conserved function to directly mediate membrane tethering, even in the absence

SUBMITTER: Inoshita M 

PROVIDER: S-EPMC5682961 | biostudies-literature | 2017 Nov

REPOSITORIES: biostudies-literature