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SNAPAP

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Template:PBB SNARE-associated protein Snapin is a protein that in humans is encoded by the SNAPIN gene.[1][2][3]

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Interactions

SNAPAP has been shown to interact with SNAP-25,[1] BLOC1S1,[4] SNAP23,[5] Dysbindin,[4] TRPV1,[6] PLDN,[4] BLOC1S2[4] and RGS7.[2]

Function

Snapin has been established to be a promoter of vesicle docking, as it plays a role in binding to SNAP-25, which together stabilize and favor SNARE complex assembly and vesicle docking.[7] Specifically, the degree to which snapin is necessary for proper synaptic release varies across species. The functions of snapin have been reported to be independent of synaptotagmin, and works through the SNAP-25 pathway to stabilize, prime, and dock vesicles.[7]

References

  1. ^ a b Ilardi JM, Mochida S, Sheng ZH (April 1999). "Snapin: a SNARE-associated protein implicated in synaptic transmission". Nat Neurosci. 2 (2): 119–24. doi:10.1038/5673. PMID 10195194.{{cite journal}}: CS1 maint: multiple names: authors list (link) Cite error: The named reference "pmid10195194" was defined multiple times with different content (see the help page).
  2. ^ a b Hunt RA, Edris W, Chanda PK, Nieuwenhuijsen B, Young KH (March 2003). "Snapin interacts with the N-terminus of regulator of G protein signaling 7". Biochem Biophys Res Commun. 303 (2): 594–9. doi:10.1016/S0006-291X(03)00400-5. PMID 12659861.{{cite journal}}: CS1 maint: multiple names: authors list (link) Cite error: The named reference "pmid12659861" was defined multiple times with different content (see the help page).
  3. ^ "Entrez Gene: SNAPAP SNAP-associated protein".
  4. ^ a b c d Starcevic, Marta (July 2004). "Identification of snapin and three novel proteins (BLOS1, BLOS2, and BLOS3/reduced pigmentation) as subunits of biogenesis of lysosome-related organelles complex-1 (BLOC-1)". J. Biol. Chem. 279 (27). United States: 28393–401. doi:10.1074/jbc.M402513200. ISSN 0021-9258. PMID 15102850. {{cite journal}}: Unknown parameter |coauthors= ignored (|author= suggested) (help)CS1 maint: unflagged free DOI (link)
  5. ^ Buxton, Penelope; Zhang Xiang-Ming; Walsh Bong; Sriratana Absorn; Schenberg Irina; Manickam Elizabeth; Rowe Tony (October 2003). "Identification and characterization of Snapin as a ubiquitously expressed SNARE-binding protein that interacts with SNAP23 in non-neuronal cells". Biochem. J. 375 (Pt 2). England: 433–40. doi:10.1042/BJ20030427. PMC 1223698. PMID 12877659.
  6. ^ Morenilla-Palao, Cruz (June 2004). "Regulated exocytosis contributes to protein kinase C potentiation of vanilloid receptor activity". J. Biol. Chem. 279 (24). United States: 25665–72. doi:10.1074/jbc.M311515200. ISSN 0021-9258. PMID 15066994. {{cite journal}}: Unknown parameter |coauthors= ignored (|author= suggested) (help)CS1 maint: unflagged free DOI (link)
  7. ^ a b Yu SC, Klosterman SM, Martin AA, Gracheva EO, Richmond JE (2013). "Differential roles for snapin and synaptotagmin in the synaptic vesicle cycle". PLoS ONE. 8 (2): e57842. doi:10.1371/journal.pone.0057842. PMC 3585204. PMID 23469084.{{cite journal}}: CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link)

Further reading

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