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A unique C2 domain at the C terminus of Munc13 promotes synaptic vesicle priming

Murugesh Padmanarayana, Haowen Liu, Francesco Michelassi, Lei Li, Daniel Betensky, Matthew J. Dominguez, R. Bryan Sutton, Zhitao Hu, Jeremy S. Dittman

2021Proceedings of the National Academy of Sciences30 citationsDOIOpen Access PDF

Abstract

Significance Rapid communication between neurons relies on the precise coordination of several presynaptic active-zone proteins. Munc13/UNC-13 is the centerpiece of this deeply conserved process, and several domains of this large cytoplasmic protein serve specific roles such as coordinating SNARE protein assembly, integrating calcium and lipid signals, and bringing synaptic vesicles close to the plasma membrane, although a mechanistic understanding of these critical steps is lacking. Here, we describe for the first time a novel C2 domain (HC2M) at the C terminus of UNC-13 that helps to bind synaptic vesicles to the plasma membrane in preparation for fusion. We demonstrate the impact of HC2M loss on nervous system function and characterize its structural, biochemical, and evolutionarily conserved features.

Topics & Concepts

Synaptic vesicleCell biologyNeurotransmissionVesicle fusionCaenorhabditis elegansBiologyVesicleKiss-and-run fusionNeurotransmitterEndosomeSignal transducing adaptor proteinC2 domainSNAP25Fusion proteinBiochemistrySignal transductionMembraneGeneReceptorRecombinant DNAIntracellularCellular transport and secretionPhotoreceptor and optogenetics researchGenetics, Aging, and Longevity in Model Organisms
A unique C2 domain at the C terminus of Munc13 promotes synaptic vesicle priming | Litcius