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A unique C2 domain at the C terminus of Munc13 promotes synaptic vesicle priming
- Source :
- Proc Natl Acad Sci U S A
- Publication Year :
- 2021
- Publisher :
- Proceedings of the National Academy of Sciences, 2021.
-
Abstract
- Neurotransmitter release during synaptic transmission comprises a tightly orchestrated sequence of molecular events, and Munc13-1 is a cornerstone of the fusion machinery. A forward genetic screen for defects in neurotransmitter release in Caenorhabditis elegans identified a mutation in the Munc13-1 ortholog UNC-13 that eliminated its unique and deeply conserved C-terminal module (referred to as HC2M) containing a Ca(2+)-insensitive C2 domain flanked by membrane-binding helices. The HC2M module could be functionally replaced in vivo by protein domains that localize to synaptic vesicles but not to the plasma membrane. HC2M is broadly conserved in other Unc13 family members and is required for efficient synaptic vesicle priming. We propose that the HC2M domain evolved as a vesicle/endosome adaptor and acquired synaptic vesicle specificity in the Unc13ABC protein family.
- Subjects :
- Protein family
Protein domain
Nerve Tissue Proteins
Neurotransmission
Synaptic Transmission
Synaptic vesicle
Exocytosis
03 medical and health sciences
chemistry.chemical_compound
0302 clinical medicine
Protein Domains
Animals
Amino Acid Sequence
Caenorhabditis elegans
Caenorhabditis elegans Proteins
Neurotransmitter
Sequence Deletion
030304 developmental biology
C2 domain
Neurotransmitter Agents
0303 health sciences
Multidisciplinary
Chemistry
Vesicle
Membrane Proteins
Biological Sciences
Cell biology
Mutation
Synaptic Vesicles
030217 neurology & neurosurgery
Synaptic vesicle priming
Subjects
Details
- ISSN :
- 10916490 and 00278424
- Volume :
- 118
- Database :
- OpenAIRE
- Journal :
- Proceedings of the National Academy of Sciences
- Accession number :
- edsair.doi.dedup.....f54cda040cb2f4e2b1f022a8f577135d