Global phosphoproteomic analysis in nerve terminal during exocytosis reveals 252 uniquely regulated phosphosites, highlighting complex regulation of active zone proteins at multiple sites and the role of specific kinases/phosphatases.
Clarinet, a novel C. elegans active zone protein with homology to vertebrate Piccolo and Rim, uses its different isoforms for diverse functions, including synaptic vesicle clustering, vesicle release and synaptogenesis.
High affinity interactions with transport adaptors are important to shield the interaction surfaces of cytomatrix components to block fatal premature oligomerization of active zone proteins during axonal transport.
A combination of tethered diffusion of release-ready synaptic vesicles and vesicle-vesicle fusion supports neurotransmitter release at the presynaptic active zone of sensory synapses.
The precise position of UNC-13 at the active zone near a synapse depends on the N-terminus of the protein, and the C2A domain in particular, and is essential for accelerating neurotransmitter release.
A novel region in the CaV2.1 α1 subunit regulates coupling of synaptic vesicles to CaV2.1 calcium channels, synaptic vesicle release and docking, and the size of the fast and total releasable pools of synaptic vesicles.
Munc13, a protein that is essential for exocytosis, controls the behavior of voltage gated calcium channels and shapes synaptic plasticity on fast time scales.
Active zone release probability is correlated with calcium channel density and calcium influx at single release sites, with release strength increasing in an activity-dependent manner during synapse maturation.
Hydrodynamic and steric interactions slow vesicle mobility and are predicted to ultimately limit vesicle supply to the active zone during sustained high-frequency signalling at a central synapse.
