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Synaptophysin

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SYP
Identifiers
AliasesSYP, MRX96, MRXsynaptophysin, XLID96
External IDsOMIM: 313475; MGI: 98467; HomoloGene: 2391; GeneCards: SYP; OMA:SYP - orthologs
Orthologs
SpeciesHumanMouse
Entrez

6855

20977

Ensembl

ENSG00000102003

ENSMUSG00000031144

UniProt

P08247

Q62277

RefSeq (mRNA)

NM_003179

NM_009305

RefSeq (protein)

NP_003170

NP_033331

Location (UCSC)Chr X: 49.19 – 49.2 MbChr X: 7.5 – 7.52 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Synaptophysin, also known as the major synaptic vesicle protein p38, is a protein that in humans is encoded by the SYP gene.[5][6]

Genomics

The gene is located on the short arm of X chromosome (Xp11.23-p11.22). It is 12,406 bases in length and lies on the minus strand. The encoded protein has 313 amino acids with a predicted molecular weight of 33.845 kDa.

Molecular biology

The protein is a synaptic vesicle glycoprotein with four transmembrane domains weighing 38kDa. It is present in neuroendocrine cells and in virtually all neurons in the brain and spinal cord that participate in synaptic transmission. It acts as a marker for neuroendocrine tumors, and its ubiquity at the synapse has led to the use of synaptophysin immunostaining for quantification of synapses.[7]

The exact function of the protein is unknown: it interacts with the essential synaptic vesicle protein synaptobrevin, but when the synaptophysin gene is experimentally inactivated in animals, they still develop and function normally.[8] Recent research has shown, however, that elimination of synaptophysin in mice creates behavioral changes such as increased exploratory behavior, impaired object novelty recognition, and reduced spatial learning.[9]

Clinical importance

This gene has been implicated in X linked intellectual disability.[10]

Using immunohistochemistry, synaptophysin can be demonstrated in a range of neural and neuroendocrine tissues,[11] including cells of the adrenal medulla and pancreatic islets. As a specific marker for these tissues, it can be used to identify tumours arising from them, such as neuroblastoma, retinoblastoma, phaeochromocytoma, carcinoid, small-cell carcinoma, medulloblastoma and medullary thyroid carcinoma, among others. Diagnostically, it is often used in combination with chromogranin A.[12]

See also

Interactions

Synaptophysin has been shown to interact with AP1G1[13] and SIAH2.[14]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000102003 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000031144 – 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. ^ "Entrez Gene: SYP synaptophysin".
  6. ^ Südhof TC, Lottspeich F, Greengard P, Mehl E, Jahn R (November 1987). "The cDNA and derived amino acid sequences for rat and human synaptophysin". Nucleic Acids Res. 15 (22): 9607. doi:10.1093/nar/15.22.9607. PMC 306499. PMID 3120152.
  7. ^ Calhoun ME, Jucker M, Martin LJ, Thinakaran G, Price DL, Mouton PR (December 1996). "Comparative evaluation of synaptophysin-based methods for quantification of synapses". J. Neurocytol. 25 (12): 821–8. doi:10.1007/BF02284844. PMID 9023727.
  8. ^ McMahon HT, Bolshakov VY, Janz R, Hammer RE, Siegelbaum SA, Südhof TC (May 1996). "Synaptophysin, a major synaptic vesicle protein, is not essential for neurotransmitter release". Proc. Natl. Acad. Sci. U.S.A. 93 (10): 4760–4. Bibcode:1996PNAS...93.4760M. doi:10.1073/pnas.93.10.4760. PMC 39352. PMID 8643476.
  9. ^ Schmitt U, Tanimoto N, Seeliger M, Schaeffel F, Leube RE (August 2009). "Detection of behavioral alterations and learning deficits in mice lacking synaptophysin". Neuroscience. 162 (2): 234–43. CiteSeerX 10.1.1.320.5309. doi:10.1016/j.neuroscience.2009.04.046. PMID 19393300.
  10. ^ Tarpey PS, Smith R, Pleasance E, Whibley A, Edkins S, Hardy C, O'Meara S, Latimer C, Dicks E, Menzies A, Stephens P, Blow M, Greenman C, Xue Y, Tyler-Smith C, Thompson D, Gray K, Andrews J, Barthorpe S, Buck G, Cole J, Dunmore R, Jones D, Maddison M, Mironenko T, Turner R, Turrell K, Varian J, West S, Widaa S, Wray P, Teague J, Butler A, Jenkinson A, Jia M, Richardson D, Shepherd R, Wooster R, Tejada MI, Martinez F, Carvill G, Goliath R, de Brouwer AP, van Bokhoven H, Van Esch H, Chelly J, Raynaud M, Ropers HH, Abidi FE, Srivastava AK, Cox J, Luo Y, Mallya U, Moon J, Parnau J, Mohammed S, Tolmie JL, Shoubridge C, Corbett M, Gardner A, Haan E, Rujirabanjerd S, Shaw M, Vandeleur L, Fullston T, Easton DF, Boyle J, Partington M, Hackett A, Field M, Skinner C, Stevenson RE, Bobrow M, Turner G, Schwartz CE, Gecz J, Raymond FL, Futreal PA, Stratton MR (May 2009). "A systematic, large-scale resequencing screen of X-chromosome coding exons in mental retardation". Nat. Genet. 41 (5): 535–43. doi:10.1038/ng.367. PMC 2872007. PMID 19377476.
  11. ^ Wiedenmann, B; Franke, WW; Kuhn, C; Moll, R; Gould, VE (May 1986). "Synaptophysin: a marker protein for neuroendocrine cells and neoplasms". Proceedings of the National Academy of Sciences of the United States of America. 83 (10): 3500–4. Bibcode:1986PNAS...83.3500W. doi:10.1073/pnas.83.10.3500. PMC 323544. PMID 3010302.
  12. ^ Leong, Anthony S-Y; Cooper, Kumarason; Leong, F Joel W-M (2003). Manual of Diagnostic Cytology (2 ed.). Greenwich Medical Media, Ltd. pp. 405–406. ISBN 978-1-84110-100-2.
  13. ^ Horikawa HP, Kneussel M, El Far O, Betz H (November 2002). "Interaction of synaptophysin with the AP-1 adaptor protein gamma-adaptin". Mol. Cell. Neurosci. 21 (3): 454–62. doi:10.1006/mcne.2002.1191. PMID 12498786.
  14. ^ Wheeler TC, Chin LS, Li Y, Roudabush FL, Li L (March 2002). "Regulation of synaptophysin degradation by mammalian homologues of seven in absentia". J. Biol. Chem. 277 (12): 10273–82. doi:10.1074/jbc.M107857200. PMID 11786535.

Further reading

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