Structure and topography of the synaptic V-ATPase-synaptophysin complex.

ABSTRACT: Synaptic vesicles are organelles with a precisely defined protein and lipid composition^1,2, yet the molecular mechanisms for the biogenesis of synaptic vesicles are mainly unknown. Here we discovered a well-defined interface between the synaptic vesicle V-ATPase and synaptophysin by in situ cryo-electron tomography and single-particle cryo-electron microscopy of functional synaptic vesicles isolated from mouse brains³. The synaptic vesicle V-ATPase is an ATP-dependent proton pump that establishes the proton gradient across the synaptic vesicle, which in turn drives the uptake of neurotransmitters^4,5. Synaptophysin⁶ and its paralogues synaptoporin⁷ and synaptogyrin⁸ belong to a family of abundant synaptic vesicle proteins who

SUBMITTER: Wang C 

PROVIDER: S-EPMC11269182 | biostudies-literature | 2024 Jul

REPOSITORIES: biostudies-literature