Amphiphysin

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Amphiphysin
PDB 1ky7 EBI.jpg
Rendering of 1KY7
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols AMPH ; AMPH1
External IDs OMIM600418 MGI103574 HomoloGene121585 GeneCards: AMPH Gene
RNA expression pattern
PBB GE AMPH 205257 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 273 218038
Ensembl ENSG00000078053 ENSMUSG00000021314
UniProt P49418 Q7TQF7
RefSeq (mRNA) NM_001635 NM_001289546
RefSeq (protein) NP_001626 NP_001276475
Location (UCSC) Chr 7:
38.42 – 38.67 Mb
Chr 13:
18.95 – 19.15 Mb
PubMed search [1] [2]

Amphiphysin is a protein that in humans is encoded by the AMPH gene.[1][2]

This gene encodes a protein associated with the cytoplasmic surface of synaptic vesicles. A subset of patients with stiff person 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.[2]

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.

Interactions[edit]

Amphiphysin has been shown to interact with DNM1,[3][4][5][6][7] Phospholipase D1,[8] CDK5R1,[9] PLD2,[8] CABIN1[10] and SH3GL2.[3][11]

See also[edit]

References[edit]

  1. ^ De Camilli, P.; Thomas, A; Cofiell, R; Folli, F; Lichte, B; Piccolo, G; Meinck, HM; Austoni, M et al. (December 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. doi:10.1084/jem.178.6.2219. PMC 2191289. PMID 8245793. 
  2. ^ a b "Entrez Gene: AMPH amphiphysin (Stiff-Man syndrome with breast cancer 128kDa autoantigen)". 
  3. ^ a b Micheva, K. D.; Kay, BK; McPherson, PS (October 1997). "Synaptojanin forms two separate complexes in the nerve terminal. Interactions with endophilin and amphiphysin". J. Biol. Chem. 272 (43): 27239–45. doi:10.1074/jbc.272.43.27239. PMID 9341169. 
  4. ^ Wigge, P; Köhler, K; Vallis, Y; Doyle, CA; Owen, D; Hunt, SP; McMahon, HT (October 1997). "Amphiphysin heterodimers: potential role in clathrin-mediated endocytosis". Mol. Biol. Cell 8 (10): 2003–15. doi:10.1091/mbc.8.10.2003. PMC 25662. PMID 9348539. 
  5. ^ McMahon, Harvey T; Wigge, Patrick; Smith, Corrin (August 1997). "Clathrin interacts specifically with amphiphysin and is displaced by dynamin". FEBS Lett. 413 (2): 319–22. doi:10.1016/S0014-5793(97)00928-9. PMID 9280305. 
  6. ^ Chen-Hwang, M.-C.; Chen, HR; Elzinga, M; Hwang, YW (May 2002). "Dynamin is a minibrain kinase/dual specificity Yak1-related kinase 1A substrate". J. Biol. Chem. 277 (20): 17597–604. doi:10.1074/jbc.M111101200. PMID 11877424. 
  7. ^ Grabs, D.; Slepnev, VI; Songyang, Z; David, C; Lynch, M; Cantley, LC; De Camilli, P (May 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. doi:10.1074/jbc.272.20.13419. PMID 9148966. 
  8. ^ a b Lee, C.; Kim, SR; Chung, JK; Frohman, MA; Kilimann, MW; Rhee, SG (June 2000). "Inhibition of phospholipase D by amphiphysins". J. Biol. Chem. 275 (25): 18751–8. doi:10.1074/jbc.M001695200. PMID 10764771. 
  9. ^ Floyd, S. R.; Porro, EB; Slepnev, VI; Ochoa, GC; Tsai, LH; De Camilli, P (March 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. 
  10. ^ Lai, M. M.; Luo, HR; Burnett, PE; Hong, JJ; Snyder, SH (November 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. 
  11. ^ Modregger, J.; Schmidt, AA; Ritter, B; Huttner, WB; Plomann, M (February 2003). "Characterization of Endophilin B1b, a brain-specific membrane-associated lysophosphatidic acid acyl transferase with properties distinct from endophilin A1". J. Biol. Chem. 278 (6): 4160–7. doi:10.1074/jbc.M208568200. PMID 12456676. 

Further reading[edit]

External links[edit]