SNAPAP

SNARE-associated protein Snapin is a protein that in humans is encoded by the SNAPIN gene.[5][6][7]

SNAPIN
Identifiers
Aliases	SNAPIN, BLOC1S7, BLOS7, SNAPAP, BORCS3, SNAP associated protein
External IDs	OMIM: 607007 MGI: 1333745 HomoloGene: 8251 GeneCards: SNAPIN
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1q21.3 Start 153,658,703 bp[1] End 153,661,852 bp[1]
Gene location (Mouse) Chr. Chromosome 3 (mouse)[2] Band 3|3 F1 Start 90,488,026 bp[2] End 90,491,033 bp[2]
Gene ontology Molecular function • GO:0001948 protein binding • SNARE binding Cellular component • cytoplasm • cytosol • membrane • synaptic vesicle • BLOC-1 complex • Golgi membrane • synapse • synaptic vesicle membrane • secretory granule • cell junction • perinuclear region of cytoplasm • cytoplasmic vesicle • axon cytoplasm • lysosome • lysosomal membrane • Golgi apparatus • BORC complex Biological process • negative regulation of neuron projection development • positive regulation of late endosome to lysosome transport • endosome to lysosome transport • synaptic vesicle exocytosis • synaptic vesicle fusion to presynaptic active zone membrane • anterograde axonal transport • melanosome organization • GO:0000046 autophagosome maturation • synaptic vesicle transport • terminal button organization • anterograde synaptic vesicle transport • intracellular protein transport • GO:0022415 viral process • neuron projection development • regulation of protein binding • synaptic vesicle maturation • GO:0010554 neurotransmitter secretion • exocytosis • chemical synaptic transmission • retrograde axonal transport • cellular protein complex localization • late endosome to lysosome transport • protein maturation • lysosomal lumen acidification • lysosome organization • lysosome localization • regulation of synaptic vesicle exocytosis Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	23557	20615
Ensembl	ENSG00000143553	ENSMUSG00000001018
UniProt	O95295	Q9Z266
RefSeq (mRNA)	NM_012437	NM_133854
RefSeq (protein)	NP_036569	NP_598615
Location (UCSC)	Chr 1: 153.66 – 153.66 Mb	Chr 3: 90.49 – 90.49 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

SNAPAP is a component of the SNARE complex of proteins that is required for synaptic vesicle docking and fusion.[5] SNAPAP is also a component of the ubiquitously expressed BLOC1 multisubunit protein complex. BLOC1 is required for normal biogenesis of specialized organelles of the endosomal-lysosomal system, such as melanosomes and platelet dense granules.[7][8]

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.[9] 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.[9]

Interactions

SNAPAP has been shown to interact with:

• BLOC1S1,[8]
• BLOC1S2,[8]
• Dysbindin,[8]
• PLDN,[8]
• RGS7,[6]
• SNAP-25,[5]
• SNAP23,[10] and
• TRPV1.[11]

References

1. GRCh38: Ensembl release 89: ENSG00000143553 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000001018 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Ilardi JM, Mochida S, Sheng ZH (Feb 1999). "Snapin: a SNARE-associated protein implicated in synaptic transmission". Nature Neuroscience. 2 (2): 119–24. doi:10.1038/5673. PMID 10195194.
6. Hunt RA, Edris W, Chanda PK, Nieuwenhuijsen B, Young KH (Apr 2003). "Snapin interacts with the N-terminus of regulator of G protein signaling 7". Biochemical and Biophysical Research Communications. 303 (2): 594–9. doi:10.1016/S0006-291X(03)00400-5. PMID 12659861.
7. "Entrez Gene: SNAPAP SNAP-associated protein".
8. Starcevic M, Dell'Angelica EC (Jul 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)". The Journal of Biological Chemistry. 279 (27): 28393–401. doi:10.1074/jbc.M402513200. PMID 15102850.
9. 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. Bibcode:2013PLoSO...857842Y. doi:10.1371/journal.pone.0057842. PMC 3585204. PMID 23469084.
10. Buxton P, Zhang XM, Walsh B, Sriratana A, Schenberg I, Manickam E, Rowe T (Oct 2003). "Identification and characterization of Snapin as a ubiquitously expressed SNARE-binding protein that interacts with SNAP23 in non-neuronal cells". The Biochemical Journal. 375 (Pt 2): 433–40. doi:10.1042/BJ20030427. PMC 1223698. PMID 12877659.
11. Morenilla-Palao C, Planells-Cases R, García-Sanz N, Ferrer-Montiel A (Jun 2004). "Regulated exocytosis contributes to protein kinase C potentiation of vanilloid receptor activity". The Journal of Biological Chemistry. 279 (24): 25665–72. doi:10.1074/jbc.M311515200. PMID 15066994.

Further reading

• Chheda MG, Ashery U, Thakur P, Rettig J, Sheng ZH (Apr 2001). "Phosphorylation of Snapin by PKA modulates its interaction with the SNARE complex". Nature Cell Biology. 3 (4): 331–8. doi:10.1038/35070000. hdl:11858/00-001M-0000-0028-9E16-7. PMID 11283605.
• Moriyama K, Bonifacino JS (Sep 2002). "Pallidin is a component of a multi-protein complex involved in the biogenesis of lysosome-related organelles". Traffic. 3 (9): 666–77. doi:10.1034/j.1600-0854.2002.30908.x. PMID 12191018.
• Ciciotte SL, Gwynn B, Moriyama K, Huizing M, Gahl WA, Bonifacino JS, Peters LL (Jun 2003). "Cappuccino, a mouse model of Hermansky-Pudlak syndrome, encodes a novel protein that is part of the pallidin-muted complex (BLOC-1)". Blood. 101 (11): 4402–7. doi:10.1182/blood-2003-01-0020. PMID 12576321.
• Battle MA, Maher VM, McCormick JJ (Jun 2003). "ST7 is a novel low-density lipoprotein receptor-related protein (LRP) with a cytoplasmic tail that interacts with proteins related to signal transduction pathways". Biochemistry. 42 (24): 7270–82. doi:10.1021/bi034081y. PMID 12809483.
• Buxton P, Zhang XM, Walsh B, Sriratana A, Schenberg I, Manickam E, Rowe T (Oct 2003). "Identification and characterization of Snapin as a ubiquitously expressed SNARE-binding protein that interacts with SNAP23 in non-neuronal cells". The Biochemical Journal. 375 (Pt 2): 433–40. doi:10.1042/BJ20030427. PMC 1223698. PMID 12877659.
• Li W, Zhang Q, Oiso N, Novak EK, Gautam R, O'Brien EP, Tinsley CL, Blake DJ, Spritz RA, Copeland NG, Jenkins NA, Amato D, Roe BA, Starcevic M, Dell'Angelica EC, Elliott RW, Mishra V, Kingsmore SF, Paylor RE, Swank RT (Sep 2003). "Hermansky-Pudlak syndrome type 7 (HPS-7) results from mutant dysbindin, a member of the biogenesis of lysosome-related organelles complex 1 (BLOC-1)". Nature Genetics. 35 (1): 84–9. doi:10.1038/ng1229. PMC 2860733. PMID 12923531.
• Morenilla-Palao C, Planells-Cases R, García-Sanz N, Ferrer-Montiel A (Jun 2004). "Regulated exocytosis contributes to protein kinase C potentiation of vanilloid receptor activity". The Journal of Biological Chemistry. 279 (24): 25665–72. doi:10.1074/jbc.M311515200. PMID 15066994.
• Starcevic M, Dell'Angelica EC (Jul 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)". The Journal of Biological Chemistry. 279 (27): 28393–401. doi:10.1074/jbc.M402513200. PMID 15102850.
• Colland F, Jacq X, Trouplin V, Mougin C, Groizeleau C, Hamburger A, Meil A, Wojcik J, Legrain P, Gauthier JM (Jul 2004). "Functional proteomics mapping of a human signaling pathway". Genome Research. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC 442148. PMID 15231748.
• Schaaf CP, Benzing J, Schmitt T, Erz DH, Tewes M, Bartram CR, Janssen JW (Feb 2005). "Novel interaction partners of the TPR/MET tyrosine kinase". FASEB Journal. 19 (2): 267–9. doi:10.1096/fj.04-1558fje. PMID 15546961.
• Rüder C, Reimer T, Delgado-Martinez I, Hermosilla R, Engelsberg A, Nehring R, Dörken B, Rehm A (Mar 2005). "EBAG9 adds a new layer of control on large dense-core vesicle exocytosis via interaction with Snapin". Molecular Biology of the Cell. 16 (3): 1245–57. doi:10.1091/mbc.E04-09-0817. PMC 551489. PMID 15635093.
• Pope SN, Lee IR (Feb 2005). "Yeast two-hybrid identification of prostatic proteins interacting with human sex hormone-binding globulin". The Journal of Steroid Biochemistry and Molecular Biology. 94 (1–3): 203–8. doi:10.1016/j.jsbmb.2005.01.007. PMID 15862967.
• Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (Sep 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070.
• Talbot K, Cho DS, Ong WY, Benson MA, Han LY, Kazi HA, Kamins J, Hahn CG, Blake DJ, Arnold SE (Oct 2006). "Dysbindin-1 is a synaptic and microtubular protein that binds brain snapin". Human Molecular Genetics. 15 (20): 3041–54. doi:10.1093/hmg/ddl246. PMID 16980328.
• Suzuki F, Morishima S, Tanaka T, Muramatsu I (Oct 2007). "Snapin, a new regulator of receptor signaling, augments alpha1A-adrenoceptor-operated calcium influx through TRPC6". The Journal of Biological Chemistry. 282 (40): 29563–73. doi:10.1074/jbc.M702063200. PMID 17684020.