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.
The presynaptic scaffolding protein Bassoon is involved in regulating neurotransmitter release by controlling synaptic vesicle pool size and vesicular protein turnover through increased ubiquitination and Parkin-dependent autophagy.
Release site heterogeneity represents a previously unknown level of structural and functional organization within individual active zones in central synapses, which determines the spatiotemporal dynamics of multi-vesicular release.
Synaptic defects previously attributed to loss of kinesin function are found to be mediated by the Wnd/DLK axonal injury signaling pathway, which restrains the total levels of presynaptic proteins in response to their accumulation.
The super-resolution fluorescence microscopy approach polarization PALM (p-PALM) reveals that macromolecular crowding and inhomogeneity within nuclear pores generate a structurally and dynamically complex permeability barrier.