Amfifizin

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Amfifizin

Prikaz baziran na 1KY7
Dostupne strukture
1KY7, 1UTC, 3SOG, 4A3A
Identifikatori
SimboliAMPH; AMPH1
Vanjski IDOMIM: 600418 MGI: 103574 HomoloGene: 121585 GeneCards: AMPH Gene
Ontologija gena
Molekularna funkcija • proteinsko vezivanje
• vezivanje proteinskog C-terminusa
• aktivnost proteinske heterodimerizacije
Celularna komponenta • citoplazma
• sinaptička vezikula
• aktinski citoskeleton
• membrana
• ćelijski spoj
• membrana sinaptičke vezikule
• citoplazmična vezikula
• aksonski terminus
• sinapsa
Biološki proces • endocitoza
• sinaptička transmisija
• učenje
• pozitivna regulacija aktivnosti GTPaze
• pozitivna regulacija endocitoze
• endocitoza sinaptičke vezikule
Pregled RNK izražavanja
podaci
Ortolozi
VrstaČovekMiš
Entrez273218038
EnsemblENSG00000078053ENSMUSG00000021314
UniProtP49418Q7TQF7
RefSeq (mRNA)NM_001635.3NM_175007.1
RefSeq (protein)NP_001626.1NP_778172.1
Lokacija (UCSC)Chr 7:
38.42 - 38.67 Mb		Chr 13:
19.04 - 19.24 Mb
PubMed pretraga[1][2]

Amfifizin je protein koji je kod ljudi kodiran AMPH genom.[1][2] Ovaj protein vezan za citoplazmnu površinu sinaptičkih vezikula. Alternativno splajsovanje gena proizvodi dve transkriptne varijante koje kodiraju različite izoforme. Dodatne splajsne varijante su opisane, ali njihove sekvence sa punom dužinom nisu određene.[2]

Amfifizin je visoko zastupljen u mozgu. On je podložan dimerizaciji. Njegov N-terminus formira interakcije sa lipidima. On sadrži membranski BAR domen, središnji domen koji vezuje klatrin i C-terminusni SH3 domen.

Primarna funkcija amfifizina u mozgu je regrutovanje dinamina na mesta klatrinom posredovane endocitoze. Dva tipa amfifizina sisara imaju sličnu strukturu. Varijanta amfifizina 2 koja ne formira interakcije sa klatrinom ili adapterom je visoko izražena u mišićnom tkivu, gde učestvuje u formiranju i stabilizaciji mreže T-tubula.

Interakcije

Poznato je da amfifizin formira interakcije sa DNM1,[3][4][5][6][7] fosfolipazom D1,[8] CDK5R1,[9] PLD2,[8] CABIN1[10] i SH3GL2.[3][11]

Reference

  1. ↑ De Camilli P., Thomas A, Cofiell R, Folli F, Lichte B, Piccolo G, Meinck HM, Austoni M, Fassetta G (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. ↑ 2,0 2,1 „Entrez Gene: AMPH amphiphysin (Stiff-Man syndrome with breast cancer 128kDa autoantigen)”. 
  3. ↑ 3,0 3,1 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. 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. ↑ 8,0 8,1 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. 

Literatura

  • Lichte B, Veh RW, Meyer HE, Kilimann MW (1992). „Amphiphysin, a novel protein associated with synaptic vesicles”. EMBO J. 11 (7): 2521–30. PMC 556727. PMID 1628617. 
  • Yamamoto Raina, Li Xu, Winter Silke, Francke Uta, Kilimann Manfred W. (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. DOI:10.1093/hmg/4.2.265. PMID 7757077. 
  • David C; Solimena, M; Decamilli, 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. DOI:10.1016/0014-5793(94)00826-4. PMID 8076697. 
  • 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. DOI:10.1073/pnas.93.1.331. PMC 40232. PMID 8552632. 
  • Grabs D.; Slepnev, VI; Songyang, Z; David, C; Lynch, M; Cantley, LC; De Camilli, P (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. 
  • Butler M. H.; David, C; Ochoa, GC; Freyberg, Z; Daniell, L; Grabs, D; Cremona, O; De Camilli, P (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. DOI:10.1083/jcb.137.6.1355. PMC 2132527. PMID 9182667. 
  • Ramjaun A. R.; Micheva, KD; Bouchelet, I; McPherson, PS (1997). „Identification and characterization of a nerve terminal-enriched amphiphysin isoform”. J. Biol. Chem. 272 (26): 16700–6. DOI:10.1074/jbc.272.26.16700. PMID 9195986. 
  • McMahon Harvey T; Wigge, Patrick; Smith, Corrin (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. 
  • Micheva Kristina D.; Ramjaun, Antoine R.; Kay, Brian K.; McPherson, Peter S. (1997). „SH3 domain-dependent interactions of endophilin with amphiphysin”. FEBS Lett. 414 (2): 308–12. DOI:10.1016/S0014-5793(97)01016-8. PMID 9315708. 
  • Wigge P; Köhler, K; Vallis, Y; Doyle, CA; Owen, D; Hunt, SP; McMahon, HT (1997). „Amphiphysin heterodimers: potential role in clathrin-mediated endocytosis”. Mol. Biol. Cell 8 (10): 2003–15. PMC 25662. PMID 9348539. 
  • Floyd S; Butler, MH; Cremona, O; David, C; Freyberg, Z; Zhang, X; Solimena, M; Tokunaga, A i dr.. (1998). „Expression of amphiphysin I, an autoantigen of paraneoplastic neurological syndromes, in breast cancer”. Mol. Med. 4 (1): 29–39. PMC 2230265. PMID 9513187. 
  • Ramjaun Antoine R.; McPherson, Peter S. (1998). „Multiple amphiphysin II splice variants display differential clathrin binding: identification of two distinct clathrin-binding sites”. J. Neurochem. 70 (6): 2369–76. DOI:10.1046/j.1471-4159.1998.70062369.x. PMID 9603201. 
  • Slepnev V. I.; Ochoa, GC; Butler, MH; Grabs, D; De Camilli, P (1998). „Role of phosphorylation in regulation of the assembly of endocytic coat complexes”. Science 281 (5378): 821–4. DOI:10.1126/science.281.5378.821. PMID 9694653. 
  • Cestra G.; Castagnoli, L; Dente, L; Minenkova, O; Petrelli, A; Migone, N; Hoffmüller, U; Schneider-Mergener, J i dr.. (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. DOI:10.1074/jbc.274.45.32001. PMID 10542231. 
  • Slepnev V. I.; 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; Frohman, MA; Kilimann, MW; Rhee, SG (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; Valtorta, F; Bongiorno Borbone, L; De Camilli, P; Greengard, P; Benfenati, F (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 M. M.; Luo, HR; Burnett, PE; Hong, JJ; Snyder, SH (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 S. R.; Porro, EB; Slepnev, VI; Ochoa, GC; Tsai, LH; De Camilli, P (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 Peter; Chow, Brenda; Stewart, Bryan A.; Iyengar, Balaji; Campos, Ana Regina; Boulianne, Gabrielle L. (2001). „Drosophila Amphiphysin is a post-synaptic protein required for normal locomotion but not endocytosis”. Traffic. 2 (11): 839–50. DOI:10.1034/j.1600-0854.2001.21113.x. PMID 11733051. 
  • Zhang Bing; Zelhof, Andrew C. (2002). „Amphiphysins: raising the BAR for synaptic vesicle recycling and membrane dynamics”. Traffic. 3 (7): 452–60. DOI:10.1034/j.1600-0854.2002.30702.x. PMID 12047553.  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. PMID 11748137. 
  • Mathew D, Popescu A, Budnik V (2003). „Drosophila amphiphysin functions during synaptic Fasciclin II membrane cycling”. J Neurosci. 23 (33): 10710–6. PMID 14627656. 

Povezano

  • AP180
  • Epsin

Spoljašnje veze

  • Amfifizin Arhivirano 2012-03-20 na Wayback Machine-u
  • De Camilli Pietro, Takei Kohji, Slepnev Vladimir I., Haucke Volker (May 1999). „Functional partnership between amphiphysin and dynamin in clathrin-mediated endocytosis”. Nat. Cell Biol. 1 (1): 33–9. DOI:10.1038/9004. PMID 10559861. 
  • Peter B. J., Kent HM, Mills IG, Vallis Y, Butler PJ, Evans PR, McMahon HT (January 2004). „BAR domains as sensors of membrane curvature: the amphiphysin BAR structure”. Science 303 (5657): 495–9. DOI:10.1126/science.1092586. PMID 14645856. 
  • Evergren Emma, Marcucci Melissa, Tomilin Nikolay, Löw Peter, Slepnev Vladimir, Andersson Fredrik, Gad Helge, Brodin Lennart, De Camilli Pietro (July 2004). „Amphiphysin is a component of clathrin coats formed during synaptic vesicle recycling at the lamprey giant synapse”. Traffic 5 (7): 514–28. DOI:10.1111/j.1398-9219.2004.00198.x. PMID 15180828. Arhivirano iz originala na datum 2013-01-05. Pristupljeno 2014-05-16. 
  • Razzaq A., Robinson IM, McMahon HT, Skepper JN, Su Y, Zelhof AC, Jackson AP, Gay NJ, O'Kane CJ (November 2001). „Amphiphysin is necessary for organization of the excitation-contraction coupling machinery of muscles, but not for synaptic vesicle endocytosis in Drosophila”. Genes Dev. 15 (22): 2967–79. DOI:10.1101/gad.207801. PMC 312829. PMID 11711432.