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CDC42

Na Galipedia, a Wikipedia en galego.
PDB 1a4r
CDC42
Identificadores
Símbolo CDC42 ; CDC42Hs; G25K
Entrez 998
OMIM

116952

RefSeq NP_001034891
UniProt P60953
Outros datos

O CDC42 ou proteína do ciclo de división celular 42 (do inglés cell division cycle 42) ou homólogo da proteína de control da división celular 42 (do inglés Cell division control protein 42 homolog)[1] é unha proteína implicada na regulación do ciclo celular. Nos humanos, o CDC42 está codificado polo xene CDC42 do cromosoma 1.[2][3]

Función

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O CDC42 humano é unha GTPase da familia Rho, que regula vías de sinalización que controlan diversas funcións celulares como a morfoloxía celular, migración, endocitose e progresión do ciclo celular. Esta proteína é moi similar ao Cdc 42 de Saccharomyces cerevisiae, e pode complementar o mutante cdc42-1 de dito lévedo. O produto do oncoxene Dbl cataliza especificamente a disociación do GDP desta proteína. Esta proteína podería regular a polimerización da actina por medio da súa unión directa á proteína da síndrome de Wiskott-Aldrich neural (N-WASP), que seguidamente activa o complexo Arp2/3. O splicing alternativo deste xene dá lugar a múltiples variantes de transcrición.[4]

Interaccións

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O CDC42 presenta interaccións con:

Notas

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  1. ↑ HomoloGene - NCBI 123986
  2. ↑ Shinjo K, Koland JG, Hart MJ, Narasimhan V, Johnson DI, Evans T, Cerione RA (December 1990). "Molecular cloning of the gene for the human placental GTP-binding protein Gp (G25K): identification of this GTP-binding protein as the human homolog of the yeast cell-division-cycle protein CDC42". Proc. Natl. Acad. Sci. U.S.A. 87 (24): 9853–7. PMC 55272. PMID 2124704. doi:10.1073/pnas.87.24.9853. 
  3. ↑ Munemitsu S, Innis MA, Clark R, McCormick F, Ullrich A, Polakis P (November 1990). "Molecular cloning and expression of a G25K cDNA, the human homolog of the yeast cell cycle gene CDC42". Mol. Cell. Biol. 10 (11): 5977–82. PMC 361395. PMID 2122236. 
  4. ↑ "Entrez Gene: CDC42 cell division cycle 42 (GTP binding protein, 25kDa)". 
  5. ↑ Walker, S J; Wu W J; Cerione R A; Brown H A (May 2000). "Activation of phospholipase D1 by Cdc42 requires the Rho insert region". J. Biol. Chem. (UNITED STATES) 275 (21): 15665–8. ISSN 0021-9258. PMID 10747870. doi:10.1074/jbc.M000076200. 
  6. ↑ 6,0 6,1 6,2 Nagata, K i; Puls A; Futter C; Aspenstrom P; Schaefer E; Nakata T; Hirokawa N; Hall A (January 1998). "The MAP kinase kinase kinase MLK2 co-localizes with activated JNK along microtubules and associates with kinesin superfamily motor KIF3". EMBO J. (ENGLAND) 17 (1): 149–58. ISSN 0261-4189. PMC 1170366. PMID 9427749. doi:10.1093/emboj/17.1.149. 
  7. ↑ Li, R; Zhang B; Zheng Y (December 1997). "Structural determinants required for the interaction between Rho GTPase and the GTPase-activating domain of p190". J. Biol. Chem. (UNITED STATES) 272 (52): 32830–5. ISSN 0021-9258. PMID 9407060. doi:10.1074/jbc.272.52.32830. 
  8. ↑ 8,0 8,1 Low, B C; Lim Y P; Lim J; Wong E S; Guy G R (November 1999). "Tyrosine phosphorylation of the Bcl-2-associated protein BNIP-2 by fibroblast growth factor receptor-1 prevents its binding to Cdc42GAP and Cdc42". J. Biol. Chem. (UNITED STATES) 274 (46): 33123–30. ISSN 0021-9258. PMID 10551883. doi:10.1074/jbc.274.46.33123. 
  9. ↑ 9,0 9,1 9,2 9,3 Zhang, B; Chernoff J; Zheng Y (April 1998). "Interaction of Rac1 with GTPase-activating proteins and putative effectors. A comparison with Cdc42 and RhoA". J. Biol. Chem. (UNITED STATES) 273 (15): 8776–82. ISSN 0021-9258. PMID 9535855. doi:10.1074/jbc.273.15.8776. 
  10. ↑ 10,0 10,1 Dan, Chuntao; Nath Niharika; Liberto Muriel; Minden Audrey (January 2002). "PAK5, a New Brain-Specific Kinase, Promotes Neurite Outgrowth in N1E-115 Cells". Mol. Cell. Biol. (United States) 22 (2): 567–77. ISSN 0270-7306. PMC 139731. PMID 11756552. doi:10.1128/MCB.22.2.567-577.2002. 
  11. ↑ Pandey, Akhilesh; Dan Ippeita, Kristiansen Troels Z, Watanabe Norinobu M, Voldby Jesper, Kajikawa Eriko, Khosravi-Far Roya, Blagoev Blagoy, Mann Matthias (May 2002). "Cloning and characterization of PAK5, a novel member of mammalian p21-activated kinase-II subfamily that is predominantly expressed in brain". Oncogene (England) 21 (24): 3939–48. ISSN 0950-9232. PMID 12032833. doi:10.1038/sj.onc.1205478. 
  12. ↑ Alberts, A S; Bouquin N; Johnston L H; Treisman R (April 1998). "Analysis of RhoA-binding proteins reveals an interaction domain conserved in heterotrimeric G protein beta subunits and the yeast response regulator protein Skn7". J. Biol. Chem. (UNITED STATES) 273 (15): 8616–22. ISSN 0021-9258. PMID 9535835. doi:10.1074/jbc.273.15.8616. 
  13. ↑ 13,0 13,1 Joberty, G; Perlungher R R; Macara I G (October 1999). "The Borgs, a New Family of Cdc42 and TC10 GTPase-Interacting Proteins". Mol. Cell. Biol. (UNITED STATES) 19 (10): 6585–97. ISSN 0270-7306. PMC 84628. PMID 10490598. 
  14. ↑ Neudauer, C L; Joberty G; Macara I G (January 2001). "PIST: a novel PDZ/coiled-coil domain binding partner for the rho-family GTPase TC10". Biochem. Biophys. Res. Commun. (United States) 280 (2): 541–7. ISSN 0006-291X. PMID 11162552. doi:10.1006/bbrc.2000.4160. 
  15. ↑ 15,0 15,1 Joberty, G; Petersen C; Gao L; Macara I G (August 2000). "The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42". Nat. Cell Biol. (ENGLAND) 2 (8): 531–9. ISSN 1465-7392. PMID 10934474. doi:10.1038/35019573. 
  16. ↑ 16,0 16,1 Noda, Y; Takeya R; Ohno S; Naito S; Ito T; Sumimoto H (February 2001). "Human homologues of the Caenorhabditis elegans cell polarity protein PAR6 as an adaptor that links the small GTPases Rac and Cdc42 to atypical protein kinase C". Genes Cells (England) 6 (2): 107–19. ISSN 1356-9597. PMID 11260256. doi:10.1046/j.1365-2443.2001.00404.x. 
  17. ↑ Makkinje, A; Quinn D A; Chen A; Cadilla C L; Force T; Bonventre J V; Kyriakis J M (June 2000). "Gene 33/Mig-6, a transcriptionally inducible adapter protein that binds GTP-Cdc42 and activates SAPK/JNK. A potential marker transcript for chronic pathologic conditions, such as diabetic nephropathy. Possible role in the response to persistent stress". J. Biol. Chem. (UNITED STATES) 275 (23): 17838–47. ISSN 0021-9258. PMID 10749885. doi:10.1074/jbc.M909735199. 
  18. ↑ Qin, Wenxin; Hu Jian, Guo Minglei, Xu Jian, Li Jinjun, Yao Genfu, Zhou Xiaomei, Jiang Huiqiu, Zhang Pingping, Shen Li, Wan Dafang, Gu Jianren (August 2003). "BNIPL-2, a novel homologue of BNIP-2, interacts with Bcl-2 and Cdc42GAP in apoptosis". Biochem. Biophys. Res. Commun. (United States) 308 (2): 379–85. ISSN 0006-291X. PMID 12901880. doi:10.1016/S0006-291X(03)01387-1. 
  19. ↑ Seoh, Mui Leng; Ng Chong Han; Yong Jeffery; Lim Louis; Leung Thomas (March 2003). "ArhGAP15, a novel human RacGAP protein with GTPase binding property". FEBS Lett. (Netherlands) 539 (1–3): 131–7. ISSN 0014-5793. PMID 12650940. doi:10.1016/S0014-5793(03)00213-8. 
  20. ↑ 20,0 20,1 Ewing, Rob M; Chu Peter, Elisma Fred, Li Hongyan, Taylor Paul, Climie Shane, McBroom-Cerajewski Linda, Robinson Mark D, O'Connor Liam, Li Michael, Taylor Rod, Dharsee Moyez, Ho Yuen, Heilbut Adrian, Moore Lynda, Zhang Shudong, Ornatsky Olga, Bukhman Yury V, Ethier Martin, Sheng Yinglun, Vasilescu Julian, Abu-Farha Mohamed, Lambert Jean-Philippe, Duewel Henry S, Stewart Ian I, Kuehl Bonnie, Hogue Kelly, Colwill Karen, Gladwish Katharine, Muskat Brenda, Kinach Robert, Adams Sally-Lin, Moran Michael F, Morin Gregg B, Topaloglou Thodoros, Figeys Daniel (2007). "Large-scale mapping of human protein–protein interactions by mass spectrometry". Mol. Syst. Biol. (England) 3 (1): 89. PMC 1847948. PMID 17353931. doi:10.1038/msb4100134. 
  21. ↑ Gorvel, J P; Chang T C; Boretto J; Azuma T; Chavrier P (January 1998). "Differential properties of D4/LyGDI versus RhoGDI: phosphorylation and rho GTPase selectivity". FEBS Lett. (NETHERLANDS) 422 (2): 269–73. ISSN 0014-5793. PMID 9490022. doi:10.1016/S0014-5793(98)00020-9. 
  22. ↑ Stevens, W K; Vranken W; Goudreau N; Xiang H; Xu P; Ni F (May 1999). "Conformation of a Cdc42/Rac interactive binding peptide in complex with Cdc42 and analysis of the binding interface". Biochemistry (UNITED STATES) 38 (19): 5968–75. ISSN 0006-2960. PMID 10320322. doi:10.1021/bi990426u. 
  23. ↑ 23,0 23,1 Abo, A; Qu J; Cammarano M S; Dan C; Fritsch A; Baud V; Belisle B; Minden A (November 1998). "PAK4, a novel effector for Cdc42Hs, is implicated in the reorganization of the actin cytoskeleton and in the formation of filopodia". EMBO J. (ENGLAND) 17 (22): 6527–40. ISSN 0261-4189. PMC 1171000. PMID 9822598. doi:10.1093/emboj/17.22.6527. 
  24. ↑ Carlier, M F; Nioche P, Broutin-L'Hermite I, Boujemaa R, Le Clainche C, Egile C, Garbay C, Ducruix A, Sansonetti P, Pantaloni D (July 2000). "GRB2 links signaling to actin assembly by enhancing interaction of neural Wiskott-Aldrich syndrome protein (N-WASp) with actin-related protein (ARP2/3) complex". J. Biol. Chem. (UNITED STATES) 275 (29): 21946–52. ISSN 0021-9258. PMID 10781580. doi:10.1074/jbc.M000687200. 
  25. ↑ Miki, H; Sasaki T; Takai Y; Takenawa T (January 1998). "Induction of filopodium formation by a WASP-related actin-depolymerizing protein N-WASP". Nature (ENGLAND) 391 (6662): 93–6. ISSN 0028-0836. PMID 9422512. doi:10.1038/34208. 
  26. ↑ Gibson, R M; Wilson-Delfosse A L (October 2001). "RhoGDI-binding-defective mutant of Cdc42Hs targets to membranes and activates filopodia formation but does not cycle with the cytosol of mammalian cells". Biochem. J. (England) 359 (Pt 2): 285–94. ISSN 0264-6021. PMC 1222146. PMID 11583574. doi:10.1042/0264-6021:3590285. 
  27. ↑ Hirsch, D S; Pirone D M; Burbelo P D (January 2001). "A new family of Cdc42 effector proteins, CEPs, function in fibroblast and epithelial cell shape changes". J. Biol. Chem. (United States) 276 (2): 875–83. ISSN 0021-9258. PMID 11035016. doi:10.1074/jbc.M007039200. 
  28. ↑ Low, B C; Seow K T; Guy G R (May 2000). "Evidence for a novel Cdc42GAP domain at the carboxyl terminus of BNIP-2". J. Biol. Chem. (UNITED STATES) 275 (19): 14415–22. ISSN 0021-9258. PMID 10799524. doi:10.1074/jbc.275.19.14415. 
  29. ↑ Low, B C; Seow K T; Guy G R (December 2000). "The BNIP-2 and Cdc42GAP homology domain of BNIP-2 mediates its homophilic association and heterophilic interaction with Cdc42GAP". J. Biol. Chem. (UNITED STATES) 275 (48): 37742–51. ISSN 0021-9258. PMID 10954711. doi:10.1074/jbc.M004897200. 
  30. ↑ Qiu, R G; Abo A; Steven Martin G (June 2000). "A human homolog of the C. elegans polarity determinant Par-6 links Rac and Cdc42 to PKCzeta signaling and cell transformation". Curr. Biol. (ENGLAND) 10 (12): 697–707. ISSN 0960-9822. PMID 10873802. doi:10.1016/S0960-9822(00)00535-2. 
  31. ↑ Brill, S; Li S; Lyman C W; Church D M; Wasmuth J J; Weissbach L; Bernards A; Snijders A J (September 1996). "The Ras GTPase-activating-protein-related human protein IQGAP2 harbors a potential actin binding domain and interacts with calmodulin and Rho family GTPases". Mol. Cell. Biol. (UNITED STATES) 16 (9): 4869–78. ISSN 0270-7306. PMC 231489. PMID 8756646. 
  32. ↑ Kuroda, S; Fukata M; Kobayashi K; Nakafuku M; Nomura N; Iwamatsu A; Kaibuchi K (September 1996). "Identification of IQGAP as a putative target for the small GTPases, Cdc42 and Rac1". J. Biol. Chem. (UNITED STATES) 271 (38): 23363–7. ISSN 0021-9258. PMID 8798539. doi:10.1074/jbc.271.38.23363. 
  33. ↑ Fukata, Masaki; Watanabe Takashi; Noritake Jun; Nakagawa Masato; Yamaga Masaki; Kuroda Shinya; Matsuura Yoshiharu; Iwamatsu Akihiro; Perez Franck; Kaibuchi Kozo (June 2002). "Rac1 and Cdc42 capture microtubules through IQGAP1 and CLIP-170". Cell (United States) 109 (7): 873–85. ISSN 0092-8674. PMID 12110184. doi:10.1016/S0092-8674(02)00800-0. 
  34. ↑ Hart, M J; Callow M G; Souza B; Polakis P (June 1996). "IQGAP1, a calmodulin-binding protein with a rasGAP-related domain, is a potential effector for cdc42Hs". EMBO J. (ENGLAND) 15 (12): 2997–3005. ISSN 0261-4189. PMC 450241. PMID 8670801. 
  35. ↑ Joyal, J L; Annan R S; Ho Y D; Huddleston M E; Carr S A; Hart M J; Sacks D B (June 1997). "Calmodulin modulates the interaction between IQGAP1 and Cdc42. Identification of IQGAP1 by nanoelectrospray tandem mass spectrometry". J. Biol. Chem. (UNITED STATES) 272 (24): 15419–25. ISSN 0021-9258. PMID 9182573. doi:10.1074/jbc.272.24.15419. 
  36. ↑ Hussain, N K; Jenna S, Glogauer M, Quinn C C, Wasiak S, Guipponi M, Antonarakis S E, Kay B K, Stossel T P, Lamarche-Vane N, McPherson P S (October 2001). "Endocytic protein intersectin-l regulates actin assembly via Cdc42 and N-WASP". Nat. Cell Biol. (England) 3 (10): 927–32. ISSN 1465-7392. PMID 11584276. doi:10.1038/ncb1001-927. 
  37. ↑ Snyder, Jason T; Worthylake David K; Rossman Kent L; Betts Laurie; Pruitt Wendy M; Siderovski David P; Der Channing J; Sondek John (June 2002). "Structural basis for the selective activation of Rho GTPases by Dbl exchange factors". Nat. Struct. Biol. (United States) 9 (6): 468–75. ISSN 1072-8368. PMID 12006984. doi:10.1038/nsb796. 
  38. ↑ Aspenström, P (July 1997). "A Cdc42 target protein with homology to the non-kinase domain of FER has a potential role in regulating the actin cytoskeleton". Curr. Biol. (ENGLAND) 7 (7): 479–87. ISSN 0960-9822. PMID 9210375. doi:10.1016/S0960-9822(06)00219-3. 
  39. ↑ 39,0 39,1 Tian, L; Nelson D L; Stewart D M (March 2000). "Cdc42-interacting protein 4 mediates binding of the Wiskott-Aldrich syndrome protein to microtubules". J. Biol. Chem. (UNITED STATES) 275 (11): 7854–61. ISSN 0021-9258. PMID 10713100. doi:10.1074/jbc.275.11.7854. 
  40. ↑ Böck, B C; Vacratsis P O; Qamirani E; Gallo K A (May 2000). "Cdc42-induced activation of the mixed-lineage kinase SPRK in vivo. Requirement of the Cdc42/Rac interactive binding motif and changes in phosphorylation". J. Biol. Chem. (UNITED STATES) 275 (19): 14231–41. ISSN 0021-9258. PMID 10799501. doi:10.1074/jbc.275.19.14231. 
  41. ↑ Soltau, Michaela; Richter Dietmar; Kreienkamp Hans-Jürgen (December 2002). "The insulin receptor substrate IRSp53 links postsynaptic shank1 to the small G-protein cdc42". Mol. Cell. Neurosci. (United States) 21 (4): 575–83. ISSN 1044-7431. PMID 12504591. doi:10.1006/mcne.2002.1201. 
  42. ↑ Krugmann, S; Jordens I; Gevaert K; Driessens M; Vandekerckhove J; Hall A (October 2001). "Cdc42 induces filopodia by promoting the formation of an IRSp53:Mena complex". Curr. Biol. (England) 11 (21): 1645–55. ISSN 0960-9822. PMID 11696321. doi:10.1016/S0960-9822(01)00506-1. 
  43. ↑ Miki, H; Yamaguchi H; Suetsugu S; Takenawa T (December 2000). "IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling". Nature (England) 408 (6813): 732–5. ISSN 0028-0836. PMID 11130076. doi:10.1038/35047107. 
  44. ↑ Kim, A S; Kakalis L T; Abdul-Manan N; Liu G A; Rosen M K (March 2000). "Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein". Nature (ENGLAND) 404 (6774): 151–8. ISSN 0028-0836. PMID 10724160. doi:10.1038/35004513. 
  45. ↑ Kolluri, R; Tolias K F; Carpenter C L; Rosen F S; Kirchhausen T (May 1996). "Direct interaction of the Wiskott-Aldrich syndrome protein with the GTPase Cdc42". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 93 (11): 5615–8. ISSN 0027-8424. PMC 39296. PMID 8643625. doi:10.1073/pnas.93.11.5615. 
  46. ↑ Symons, M; Derry J M; Karlak B; Jiang S; Lemahieu V; Mccormick F; Francke U; Abo A (March 1996). "Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization". Cell (UNITED STATES) 84 (5): 723–34. ISSN 0092-8674. PMID 8625410. doi:10.1016/S0092-8674(00)81050-8. 
  47. ↑ Nakazawa, Takanobu; Watabe Ayako M; Tezuka Tohru; Yoshida Yutaka; Yokoyama Kazumasa; Umemori Hisashi; Inoue Akihiro; Okabe Shigeo; Manabe Toshiya; Yamamoto Tadashi (July 2003). "p250GAP, a Novel Brain-enriched GTPase-activating Protein for Rho Family GTPases, Is Involved in the N-Methyl-d-aspartate Receptor Signaling". Mol. Biol. Cell (United States) 14 (7): 2921–34. ISSN 1059-1524. PMC 165687. PMID 12857875. doi:10.1091/mbc.E02-09-0623. 
  48. ↑ Zhao, Chunmei; Ma Hong, Bossy-Wetzel Ella, Lipton Stuart A, Zhang Zhuohua, Feng Gen-Sheng (September 2003). "GC-GAP, a Rho family GTPase-activating protein that interacts with signaling adapters Gab1 and Gab2". J. Biol. Chem. (United States) 278 (36): 34641–53. ISSN 0021-9258. PMID 12819203. doi:10.1074/jbc.M304594200. 
  49. ↑ Nakamura, Takeshi; Komiya Misako; Sone Kiyoaki; Hirose Eiji; Gotoh Noriko; Morii Hiroshi; Ohta Yasutaka; Mori Nozomu (December 2002). "Grit, a GTPase-Activating Protein for the Rho Family, Regulates Neurite Extension through Association with the TrkA Receptor and N-Shc and CrkL/Crk Adapter Molecules". Mol. Cell. Biol. (United States) 22 (24): 8721–34. ISSN 0270-7306. PMC 139861. PMID 12446789. doi:10.1128/MCB.22.24.8721-8734.2002. 

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