Amphiphysin

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AMPH
PDB 1ky7 EBI.jpg
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases AMPH, AMPH1, amphiphysin
External IDs OMIM: 600418 MGI: 103574 HomoloGene: 121585 GeneCards: AMPH
RNA expression pattern
PBB GE AMPH 205257 s at fs.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001635
NM_139316

NM_175007
NM_001289546

RefSeq (protein)

NP_001626
NP_647477

NP_001276475.1
NP_778172.1
NP_001276475
NP_778172

Location (UCSC) Chr 7: 38.38 – 38.63 Mb Chr 13: 18.95 – 19.15 Mb
PubMed search [1] [2]
Wikidata
View/Edit Human View/Edit Mouse

Amphiphysin is a protein that in humans is encoded by the AMPH gene.[3][4]

Function[edit]

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.[4]

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,[5][6][7][8][9] Phospholipase D1,[10] CDK5R1,[11] PLD2,[10] CABIN1[12] and SH3GL2.[5][13]

See also[edit]

References[edit]

  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ 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". The Journal of Experimental Medicine. 178 (6): 2219–23. doi:10.1084/jem.178.6.2219. PMC 2191289Freely accessible. PMID 8245793. 
  4. ^ a b "Entrez Gene: AMPH amphiphysin (Stiff-Man syndrome with breast cancer 128kDa autoantigen)". 
  5. ^ a b Micheva KD, Kay BK, McPherson PS (October 1997). "Synaptojanin forms two separate complexes in the nerve terminal. Interactions with endophilin and amphiphysin". The Journal of Biological Chemistry. 272 (43): 27239–45. doi:10.1074/jbc.272.43.27239. PMID 9341169. 
  6. ^ Wigge P, Köhler K, Vallis Y, Doyle CA, Owen D, Hunt SP, McMahon HT (October 1997). "Amphiphysin heterodimers: potential role in clathrin-mediated endocytosis". Molecular Biology of the Cell. 8 (10): 2003–15. doi:10.1091/mbc.8.10.2003. PMC 25662Freely accessible. PMID 9348539. 
  7. ^ McMahon HT, Wigge P, Smith C (August 1997). "Clathrin interacts specifically with amphiphysin and is displaced by dynamin". FEBS Letters. 413 (2): 319–22. doi:10.1016/S0014-5793(97)00928-9. PMID 9280305. 
  8. ^ Chen-Hwang MC, Chen HR, Elzinga M, Hwang YW (May 2002). "Dynamin is a minibrain kinase/dual specificity Yak1-related kinase 1A substrate". The Journal of Biological Chemistry. 277 (20): 17597–604. doi:10.1074/jbc.M111101200. PMID 11877424. 
  9. ^ 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". The Journal of Biological Chemistry. 272 (20): 13419–25. doi:10.1074/jbc.272.20.13419. PMID 9148966. 
  10. ^ a b Lee C, Kim SR, Chung JK, Frohman MA, Kilimann MW, Rhee SG (June 2000). "Inhibition of phospholipase D by amphiphysins". The Journal of Biological Chemistry. 275 (25): 18751–8. doi:10.1074/jbc.M001695200. PMID 10764771. 
  11. ^ Floyd SR, 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". The Journal of Biological Chemistry. 276 (11): 8104–10. doi:10.1074/jbc.M008932200. PMID 11113134. 
  12. ^ Lai MM, Luo HR, Burnett PE, Hong JJ, Snyder SH (November 2000). "The calcineurin-binding protein cain is a negative regulator of synaptic vesicle endocytosis". The Journal of Biological Chemistry. 275 (44): 34017–20. doi:10.1074/jbc.C000429200. PMID 10931822. 
  13. ^ 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". The Journal of Biological Chemistry. 278 (6): 4160–7. doi:10.1074/jbc.M208568200. PMID 12456676. 

Further reading[edit]

External links[edit]