Amphiphysin

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Amphiphysin (Stiff-Man syndrome with breast cancer 128kDa autoantigen)
Identifiers
Symbol(s) AMPH; AMPH1
External IDs OMIM: 600418 MGI: 103574 HomoloGene: 36072
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 273 218038
Ensembl ENSG00000078053 ENSMUSG00000021314
Uniprot P49418 Q80YA2
Refseq NM_001635 (mRNA)
NP_001626 (protein)		 NM_175007 (mRNA)
NP_778172 (protein)
Location Chr 7: 38.39 - 38.64 Mb Chr 13: 18.96 - 19.16 Mb
Pubmed search [1] [2]

Amphiphysin (Stiff-Man syndrome with breast cancer 128kDa autoantigen), also known as AMPH, is a human gene.[1]

This gene encodes a protein associated with the cytoplasmic surface of synaptic vesicles. A subset of patients with stiff-man syndrome who were also affected by breast cancer are positive for autoantibodies against this protein. Alternate splicing of this gene results in two transcript variants encoding different isoforms. Additional splice variants have been described, but their full length sequences have not been determined.[1]

Amphiphysin is a brain-enriched protein with an N-terminal lipid interaction, dimerisation and membrane bending BAR domain, a middle clathrin and adaptor binding domain and a C-terminal SH3 domain. In the brain, its primary function is thought to be the recruitment of dynamin to sites of clathrin-mediated endocytosis. There are 2 mammalian amphiphysins with similar overall structure. A ubiquitous splice form of amphiphysin 2 that does not contain clathrin or adaptor interactions is highly expressed in muscle tissue and is involved in the formation and stabilization of the T-tubule network. In other tissues amphiphysin is likely involved in other membrane bending and curvature stabilization events.

Contents

[edit] See also

[edit] References

  1. ^ a b Entrez Gene: AMPH amphiphysin (Stiff-Man syndrome with breast cancer 128kDa autoantigen).

[edit] Further reading

  • Lichte B, Veh RW, Meyer HE, Kilimann MW (1992). "Amphiphysin, a novel protein associated with synaptic vesicles.". EMBO J. 11 (7): 2521–30. PMID 1628617. 
  • Yamamoto R, Li X, Winter S, et al. (1995). "Primary structure of human amphiphysin, the dominant autoantigen of paraneoplastic stiff-man syndrome, and mapping of its gene (AMPH) to chromosome 7p13-p14.". Hum. Mol. Genet. 4 (2): 265–8. PMID 7757077. 
  • David C, Solimena M, De Camilli P (1994). "Autoimmunity in stiff-Man syndrome with breast cancer is targeted to the C-terminal region of human amphiphysin, a protein similar to the yeast proteins, Rvs167 and Rvs161.". FEBS Lett. 351 (1): 73–9. PMID 8076697. 
  • De Camilli P, Thomas A, Cofiell R, et al. (1993). "The synaptic vesicle-associated protein amphiphysin is the 128-kD autoantigen of Stiff-Man syndrome with breast cancer.". J. Exp. Med. 178 (6): 2219–23. PMID 8245793. 
  • David C, McPherson PS, Mundigl O, de Camilli P (1996). "A role of amphiphysin in synaptic vesicle endocytosis suggested by its binding to dynamin in nerve terminals.". Proc. Natl. Acad. Sci. U.S.A. 93 (1): 331–5. PMID 8552632. 
  • Grabs D, Slepnev VI, Songyang Z, et al. (1997). "The SH3 domain of amphiphysin binds the proline-rich domain of dynamin at a single site that defines a new SH3 binding consensus sequence.". J. Biol. Chem. 272 (20): 13419–25. PMID 9148966. 
  • Butler MH, David C, Ochoa GC, et al. (1997). "Amphiphysin II (SH3P9; BIN1), a member of the amphiphysin/Rvs family, is concentrated in the cortical cytomatrix of axon initial segments and nodes of ranvier in brain and around T tubules in skeletal muscle.". J. Cell Biol. 137 (6): 1355–67. PMID 9182667. 
  • Ramjaun AR, Micheva KD, Bouchelet I, McPherson PS (1997). "Identification and characterization of a nerve terminal-enriched amphiphysin isoform.". J. Biol. Chem. 272 (26): 16700–6. PMID 9195986. 
  • McMahon HT, Wigge P, Smith C (1997). "Clathrin interacts specifically with amphiphysin and is displaced by dynamin.". FEBS Lett. 413 (2): 319–22. PMID 9280305. 
  • Micheva KD, Ramjaun AR, Kay BK, McPherson PS (1997). "SH3 domain-dependent interactions of endophilin with amphiphysin.". FEBS Lett. 414 (2): 308–12. PMID 9315708. 
  • Wigge P, Köhler K, Vallis Y, et al. (1997). "Amphiphysin heterodimers: potential role in clathrin-mediated endocytosis.". Mol. Biol. Cell 8 (10): 2003–15. PMID 9348539. 
  • Floyd S, Butler MH, Cremona O, et al. (1998). "Expression of amphiphysin I, an autoantigen of paraneoplastic neurological syndromes, in breast cancer.". Mol. Med. 4 (1): 29–39. PMID 9513187. 
  • Ramjaun AR, McPherson PS (1998). "Multiple amphiphysin II splice variants display differential clathrin binding: identification of two distinct clathrin-binding sites.". J. Neurochem. 70 (6): 2369–76. PMID 9603201. 
  • Slepnev VI, Ochoa GC, Butler MH, et al. (1998). "Role of phosphorylation in regulation of the assembly of endocytic coat complexes.". Science 281 (5378): 821–4. PMID 9694653. 
  • Cestra G, Castagnoli L, Dente L, et al. (1999). "The SH3 domains of endophilin and amphiphysin bind to the proline-rich region of synaptojanin 1 at distinct sites that display an unconventional binding specificity.". J. Biol. Chem. 274 (45): 32001–7. PMID 10542231. 
  • Slepnev VI, Ochoa GC, Butler MH, De Camilli P (2000). "Tandem arrangement of the clathrin and AP-2 binding domains in amphiphysin 1 and disruption of clathrin coat function by amphiphysin fragments comprising these sites.". J. Biol. Chem. 275 (23): 17583–9. doi:10.1074/jbc.M910430199. PMID 10748223. 
  • Lee C, Kim SR, Chung JK, et al. (2000). "Inhibition of phospholipase D by amphiphysins.". J. Biol. Chem. 275 (25): 18751–8. doi:10.1074/jbc.M001695200. PMID 10764771. 
  • Onofri F, Giovedi S, Kao HT, et al. (2000). "Specificity of the binding of synapsin I to Src homology 3 domains.". J. Biol. Chem. 275 (38): 29857–67. doi:10.1074/jbc.M006018200. PMID 10899172. 
  • Lai MM, Luo HR, Burnett PE, et al. (2000). "The calcineurin-binding protein cain is a negative regulator of synaptic vesicle endocytosis.". J. Biol. Chem. 275 (44): 34017–20. doi:10.1074/jbc.C000429200. PMID 10931822. 
  • Floyd SR, Porro EB, Slepnev VI, et al. (2001). "Amphiphysin 1 binds the cyclin-dependent kinase (cdk) 5 regulatory subunit p35 and is phosphorylated by cdk5 and cdc2.". J. Biol. Chem. 276 (11): 8104–10. doi:10.1074/jbc.M008932200. PMID 11113134. 
  • Leventis PA, Chow BM, Stewart BA, Iyengar B, Campos AR, Boulianne GL. (2001). Drosophila Amphiphysin is a post-synaptic protein required for normal locomotion but not endocytosis. Traffic. 2(11):839-50.
  • Zhang B, Zelhof AC. (2002). Amphiphysins: raising the BAR for synaptic vesicle recycling and membrane dynamics. Traffic. 3(7):452-60. Review.
  • Zelhof AC, Bao H, Hardy RW, Razzaq A, Zhang B, Doe CQ. (2001). Drosophila Amphiphysin is implicated in protein localization and membrane morphogenesis but not in synaptic vesicle endocytosis. Development. 128(24):5005-15.
  • Mathew D, Popescu A, Budnik V. (2003). Drosophila amphiphysin functions during synaptic Fasciclin II membrane cycling. J Neurosci. 23(33):10710-6.

[edit] External links

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