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CD2AP

Na Galipedia, a Wikipedia en galego.
PDB 2j6f
Proteína asociada a CD2
Identificadores
Símbolo CD2AP; CMS
Entrez 23607
HUGO 7663
OMIM

604241

RefSeq NP_036252
UniProt Q9Y5K6
Outros datos
Locus Cr. 6 :(47.48 – 47.63 Mb)

A proteína asociada a CD2 (CD2AP) é unha proteína que nos humanos está codificada polo xene CD2AP situado no cromosoma 6, que intervén no funcionamento do citoesqueleto.[1][2]

Función

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Este xene codifica unha molécula de armazón que regula o citoesqueleto de actina. A proteína interacciona directamente coa actina filamentosa e unha variedade de proteínas da membrana celular por medio de múltiples sitios de unión á actina, dominios SH3, e unha rexión rica en prolina que contén sitios de unión para os dominios SH3. A proteína citoplásmica localízase en pregamentos da membrana, balsas lipídicas, e os bordos anteriores das células en avance. Está implicada na remodelación da actina dinámica e no tráfico de membrana que ocorre durante a endocitose mediada por receptor e a citocinese. A haploinsuficiencia deste xene está implicada na susceptibilidade a enfermidades glomerulares.[2]

Interaccións

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A proteína CD2AP presenta interaccións con:

Notas

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  1. ↑ Kirsch KH, Georgescu MM, Ishimaru S, Hanafusa H (Jun 1999). "CMS: An adapter molecule involved in cytoskeletal rearrangements". Proc Natl Acad Sci USA 96 (11): 6211–6. PMC 26861. PMID 10339567. doi:10.1073/pnas.96.11.6211. 
  2. ↑ 2,0 2,1 "Entrez Gene: CD2AP CD2-associated protein". 
  3. ↑ Haglund K, Ivankovic-Dikic I, Shimokawa N, Kruh GD, Dikic I (May 2004). "Recruitment of Pyk2 and Cbl to lipid rafts mediates signals important for actin reorganization in growing neurites". J. Cell. Sci. 117 (Pt 12): 2557–68. PMID 15128873. doi:10.1242/jcs.01148. 
  4. ↑ Kirsch KH, Georgescu MM, Shishido T, Langdon WY, Birge RB, Hanafusa H (Feb 2001). "The adapter type protein CMS/CD2AP binds to the proto-oncogenic protein c-Cbl through a tyrosine phosphorylation-regulated Src homology 3 domain interaction". J. Biol. Chem. 276 (7): 4957–63. PMID 11067845. doi:10.1074/jbc.M005784200. 
  5. ↑ 5,0 5,1 Cormont M, Metón I, Mari M, Monzo P, Keslair F, Gaskin C, McGraw TE, Le Marchand-Brustel Y (Feb 2003). "CD2AP/CMS regulates endosome morphology and traffic to the degradative pathway through its interaction with Rab4 and c-Cbl". Traffic 4 (2): 97–112. PMID 12559036. doi:10.1034/j.1600-0854.2003.40205.x. 
  6. ↑ Schwarz K, Simons M, Reiser J, Saleem MA, Faul C, Kriz W, Shaw AS, Holzman LB, Mundel P (Dec 2001). "Podocin, a raft-associated component of the glomerular slit diaphragm, interacts with CD2AP and nephrin". J. Clin. Invest. 108 (11): 1621–9. PMC 200981. PMID 11733557. doi:10.1172/JCI12849. 
  7. ↑ Lehtonen S, Lehtonen E, Kudlicka K, Holthöfer H, Farquhar MG (Sep 2004). "Nephrin forms a complex with adherens junction proteins and CASK in podocytes and in Madin-Darby canine kidney cells expressing nephrin". Am. J. Pathol. 165 (3): 923–36. PMC 1618613. PMID 15331416. doi:10.1016/S0002-9440(10)63354-8. 

Véxase tamén

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Outros artigos

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Bibliografía

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  • Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. PMID 8889548. doi:10.1101/gr.6.9.791. 
  • Dustin ML, Olszowy MW, Holdorf AD, Li J, Bromley S, Desai N, Widder P, Rosenberger F, van der Merwe PA, Allen PM, Shaw AS (1998). "A novel adaptor protein orchestrates receptor patterning and cytoskeletal polarity in T-cell contacts". Cell 94 (5): 667–77. PMID 9741631. doi:10.1016/S0092-8674(00)81608-6. 
  • Lehtonen S, Ora A, Olkkonen VM, Geng L, Zerial M, Somlo S, Lehtonen E (2000). "In vivo interaction of the adapter protein CD2-associated protein with the type 2 polycystic kidney disease protein, polycystin-2". J. Biol. Chem. 275 (42): 32888–93. PMID 10913159. doi:10.1074/jbc.M006624200. 
  • Li C, Ruotsalainen V, Tryggvason K, Shaw AS, Miner JH (2000). "CD2AP is expressed with nephrin in developing podocytes and is found widely in mature kidney and elsewhere". Am. J. Physiol. Renal Physiol. 279 (4): F785–92. PMID 10997929. 
  • Kirsch KH, Georgescu MM, Shishido T, Langdon WY, Birge RB, Hanafusa H (2001). "The adapter type protein CMS/CD2AP binds to the proto-oncogenic protein c-Cbl through a tyrosine phosphorylation-regulated Src homology 3 domain interaction". J. Biol. Chem. 276 (7): 4957–63. PMID 11067845. doi:10.1074/jbc.M005784200. 
  • Schwarz K, Simons M, Reiser J, Saleem MA, Faul C, Kriz W, Shaw AS, Holzman LB, Mundel P (2002). "Podocin, a raft-associated component of the glomerular slit diaphragm, interacts with CD2AP and nephrin". J. Clin. Invest. 108 (11): 1621–9. PMC 200981. PMID 11733557. doi:10.1172/JCI12849. 
  • Scott MP, Zappacosta F, Kim EY, Annan RS, Miller WT (2002). "Identification of novel SH3 domain ligands for the Src family kinase Hck. Wiskott-Aldrich syndrome protein (WASP), WASP-interacting protein (WIP), and ELMO1". J. Biol. Chem. 277 (31): 28238–46. PMID 12029088. doi:10.1074/jbc.M202783200. 
  • Badour K, Zhang J, Shi F, McGavin MK, Rampersad V, Hardy LA, Field D, Siminovitch KA (2003). "The Wiskott-Aldrich syndrome protein acts downstream of CD2 and the CD2AP and PSTPIP1 adaptors to promote formation of the immunological synapse". Immunity 18 (1): 141–54. PMID 12530983. doi:10.1016/S1074-7613(02)00516-2. 
  • Cormont M, Metón I, Mari M, Monzo P, Keslair F, Gaskin C, McGraw TE, Le Marchand-Brustel Y (2003). "CD2AP/CMS regulates endosome morphology and traffic to the degradative pathway through its interaction with Rab4 and c-Cbl". Traffic 4 (2): 97–112. PMID 12559036. doi:10.1034/j.1600-0854.2003.40205.x. 
  • Lynch DK, Winata SC, Lyons RJ, Hughes WE, Lehrbach GM, Wasinger V, Corthals G, Cordwell S, Daly RJ (2003). "A Cortactin-CD2-associated protein (CD2AP) complex provides a novel link between epidermal growth factor receptor endocytosis and the actin cytoskeleton". J. Biol. Chem. 278 (24): 21805–13. PMID 12672817. doi:10.1074/jbc.M211407200. 
  • Hutchings NJ, Clarkson N, Chalkley R, Barclay AN, Brown MH (2003). "Linking the T cell surface protein CD2 to the actin-capping protein CAPZ via CMS and CIN85". J. Biol. Chem. 278 (25): 22396–403. PMID 12690097. doi:10.1074/jbc.M302540200. 
  • Kim JM, Wu H, Green G, Winkler CA, Kopp JB, Miner JH, Unanue ER, Shaw AS (2003). "CD2-associated protein haploinsufficiency is linked to glomerular disease susceptibility". Science 300 (5623): 1298–300. PMID 12764198. doi:10.1126/science.1081068. 
  • Schulze WX, Mann M (2004). "A novel proteomic screen for peptide-protein interactions". J. Biol. Chem. 279 (11): 10756–64. PMID 14679214. doi:10.1074/jbc.M309909200. 
  • Haglund K, Ivankovic-Dikic I, Shimokawa N, Kruh GD, Dikic I (2004). "Recruitment of Pyk2 and Cbl to lipid rafts mediates signals important for actin reorganization in growing neurites". J. Cell. Sci. 117 (Pt 12): 2557–68. PMID 15128873. doi:10.1242/jcs.01148. 
  • Lehtonen S, Lehtonen E, Kudlicka K, Holthöfer H, Farquhar MG (2004). "Nephrin Forms a Complex with Adherens Junction Proteins and CASK in Podocytes and in Madin-Darby Canine Kidney Cells Expressing Nephrin". Am. J. Pathol. 165 (3): 923–36. PMC 1618613. PMID 15331416. doi:10.1016/S0002-9440(10)63354-8. 
  • Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ (2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". Nat. Biotechnol. 23 (1): 94–101. PMID 15592455. doi:10.1038/nbt1046. 
  • Coward RJ, Foster RR, Patton D, Ni L, Lennon R, Bates DO, Harper SJ, Mathieson PW, Saleem MA (2005). "Nephrotic plasma alters slit diaphragm-dependent signaling and translocates nephrin, Podocin, and CD2 associated protein in cultured human podocytes". J. Am. Soc. Nephrol. 16 (3): 629–37. PMID 15659563. doi:10.1681/ASN.2004030172. 
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