Cryo-electron tomography reveals a critical role of RIM1α in synaptic vesicle tethering.

ABSTRACT: Synaptic vesicles are embedded in a complex filamentous network at the presynaptic terminal. Before fusion, vesicles are linked to the active zone (AZ) by short filaments (tethers). The identity of the molecules that form and regulate tethers remains unknown, but Rab3-interacting molecule (RIM) is a prominent candidate, given its central role in AZ organization. In this paper, we analyzed presynaptic architecture of RIM1α knockout (KO) mice by cryo-electron tomography. In stark contrast to previous work on dehydrated, chemically fixed samples, our data show significant alterations in vesicle distribution and AZ tethering that could provide a structural basis for the functional deficits of RIM1α KO synapses. Proteasome inhibition reversed these structural defects, suggesting a functional re

SUBMITTER: Fernandez-Busnadiego R 

PROVIDER: S-EPMC3664715 | biostudies-literature | 2013 May

REPOSITORIES: biostudies-literature