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Rabphilin regulates SNARE-dependent re-priming of synaptic vesicles for fusion.

Authors: Deak, F  Shin, OH  Tang, J  Hanson, P  Ubach, J  Jahn, R  Rizo, J  Kavalali, ET  Sudhof, TC 
Citation: Deak F, etal., EMBO J. 2006 Jun 21;25(12):2856-66. Epub 2006 Jun 8.
Pubmed: (View Article at PubMed) PMID:16763567
DOI: Full-text: DOI:10.1038/sj.emboj.7601165

Synaptic vesicle fusion is catalyzed by assembly of synaptic SNARE complexes, and is regulated by the synaptic vesicle GTP-binding protein Rab3 that binds to RIM and to rabphilin. RIM is a known physiological regulator of fusion, but the role of rabphilin remains obscure. We now show that rabphilin regulates recovery of synaptic vesicles from use-dependent depression, probably by a direct interaction with the SNARE protein SNAP-25. Deletion of rabphilin dramatically accelerates recovery of depressed synaptic responses; this phenotype is rescued by viral expression of wild-type rabphilin, but not of mutant rabphilin lacking the second rabphilin C2 domain that binds to SNAP-25. Moreover, deletion of rabphilin also increases the size of synaptic responses in synapses lacking the vesicular SNARE protein synaptobrevin in which synaptic responses are severely depressed. Our data suggest that binding of rabphilin to SNAP-25 regulates exocytosis of synaptic vesicles after the readily releasable pool has either been physiologically exhausted by use-dependent depression, or has been artificially depleted by deletion of synaptobrevin.

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CRRD Object Information
CRRD ID: 8553578
Created: 2014-05-08
Species: All species
Last Modified: 2014-05-08
Status: ACTIVE



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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.