CDC42

A CDC42 ou proteína do ciclo de divisão celular 42 (do inglês cell division cycle 42) ou homólogo da proteína de controlo da divisão celular 42 (do inglês Cell division control protein 42 homolog)[1] é uma proteína implicada na regulação do ciclo celular. Nos humanos, a CDC42 é codificada pelo gene CDC42 no cromossoma 1.[2][3]

Função

A CDC42 humana é uma GTPase da família Rho, que regula vias de sinalização que controlam diversas funções celulares como a morfologia celular, migração, endocitose e progressão do ciclo celular. Esta proteína é muito semelhante à Cdc42 de Saccharomyces cerevisiae, e pode complementar o mutante cdc42-1 da referida levedura. O produto do oncogene Dbl catalisa especificamente a dissociação do GDP desta proteína. Esta proteína poderia regular a polimerização da actina por meio da sua ligação direta à proteína da síndrome de Wiskott-Aldrich neural (N-WASP), que seguidamente ativa o complexo Arp2/3. O splicing alternativo deste gene dá lugar a múltiplas variantes de transcrição.[4]

Interações

A CDC42 apresenta interações com:

Referências

  1. ↑ HomoloGene - NCBI 123986
  2. ↑ Shinjo K, Koland JG, Hart MJ, Narasimhan V, Johnson DI, Evans T, Cerione RA (Dezembro de 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 55272Acessível livremente. PMID 2124704. doi:10.1073/pnas.87.24.9853 
  3. ↑ Munemitsu S, Innis MA, Clark R, McCormick F, Ullrich A, Polakis P (Novembro de 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 361395Acessível livremente. PMID 2122236. doi:10.1128/mcb.10.11.5977-5982.1990 
  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 (Maio de 2000). «Activation of phospholipase D1 by Cdc42 requires the Rho insert region». J. Biol. Chem. 275 (21): 15665–8. PMID 10747870. doi:10.1074/jbc.M000076200 
  6. ↑ a b c Nagata, K i; Puls A; Futter C; Aspenstrom P; Schaefer E; Nakata T; Hirokawa N; Hall A (Janeiro de 1998). «The MAP kinase kinase kinase MLK2 co-localizes with activated JNK along microtubules and associates with kinesin superfamily motor KIF3». EMBO J. 17 (1): 149–58. PMC 1170366Acessível livremente. PMID 9427749. doi:10.1093/emboj/17.1.149 
  7. ↑ Li, R; Zhang B; Zheng Y (Dezembro de 1997). «Structural determinants required for the interaction between Rho GTPase and the GTPase-activating domain of p190». J. Biol. Chem. 272 (52): 32830–5. PMID 9407060. doi:10.1074/jbc.272.52.32830 
  8. ↑ a b Low, B C; Lim Y P; Lim J; Wong E S; Guy G R (Novembro de 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. 274 (46): 33123–30. PMID 10551883. doi:10.1074/jbc.274.46.33123 
  9. ↑ a b c d Zhang, B; Chernoff J; Zheng Y (Abril de 1998). «Interaction of Rac1 with GTPase-activating proteins and putative effectors. A comparison with Cdc42 and RhoA». J. Biol. Chem. 273 (15): 8776–82. PMID 9535855. doi:10.1074/jbc.273.15.8776 
  10. ↑ a b Dan, Chuntao; Nath Niharika; Liberto Muriel; Minden Audrey (Janeiro de 2002). «PAK5, a New Brain-Specific Kinase, Promotes Neurite Outgrowth in N1E-115 Cells». Mol. Cell. Biol. 22 (2): 567–77. PMC 139731Acessível livremente. 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 (Maio de 2002). «Cloning and characterization of PAK5, a novel member of mammalian p21-activated kinase-II subfamily that is predominantly expressed in brain». Oncogene. 21 (24): 3939–48. PMID 12032833. doi:10.1038/sj.onc.1205478 
  12. ↑ Alberts, A S; Bouquin N; Johnston L H; Treisman R (Abril de 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. 273 (15): 8616–22. PMID 9535835. doi:10.1074/jbc.273.15.8616 
  13. ↑ a b Joberty, G; Perlungher R R; Macara I G (Outubro de 1999). «The Borgs, a New Family of Cdc42 and TC10 GTPase-Interacting Proteins». Mol. Cell. Biol. 19 (10): 6585–97. PMC 84628Acessível livremente. PMID 10490598. doi:10.1128/MCB.19.10.6585 
  14. ↑ Neudauer, C L; Joberty G; Macara I G (Janeiro de 2001). «PIST: a novel PDZ/coiled-coil domain binding partner for the rho-family GTPase TC10». Biochem. Biophys. Res. Commun. 280 (2): 541–7. PMID 11162552. doi:10.1006/bbrc.2000.4160 
  15. ↑ a b Joberty, G; Petersen C; Gao L; Macara I G (Agosto de 2000). «The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42». Nat. Cell Biol. 2 (8): 531–9. PMID 10934474. doi:10.1038/35019573 
  16. ↑ a b Noda, Y; Takeya R; Ohno S; Naito S; Ito T; Sumimoto H (Fevereiro de 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. 6 (2): 107–19. 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 (Junho de 2000). «Gene 33/Mig-6, a transcriptionally inducible adapter protein that binds GTP-Cdc42 and activates SAPK/JNK». J. Biol. Chem. 275 (23): 17838–47. 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 (Agosto de 2003). «BNIPL-2, a novel homologue of BNIP-2, interacts with Bcl-2 and Cdc42GAP in apoptosis». Biochem. Biophys. Res. Commun. 308 (2): 379–85. PMID 12901880. doi:10.1016/S0006-291X(03)01387-1 
  19. ↑ Seoh, Mui Leng; Ng Chong Han; Yong Jeffery; Lim Louis; Leung Thomas (Março de 2003). «ArhGAP15, a novel human RacGAP protein with GTPase binding property». FEBS Lett. 539 (1–3): 131–7. PMID 12650940. doi:10.1016/S0014-5793(03)00213-8 
  20. ↑ a b 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. 3 (1). 89 páginas. PMC 1847948Acessível livremente. PMID 17353931. doi:10.1038/msb4100134 
  21. ↑ Gorvel, J P; Chang T C; Boretto J; Azuma T; Chavrier P (Janeiro de 1998). «Differential properties of D4/LyGDI versus RhoGDI: phosphorylation and rho GTPase selectivity». FEBS Lett. 422 (2): 269–73. PMID 9490022. doi:10.1016/S0014-5793(98)00020-9 
  22. ↑ Stevens, W K; Vranken W; Goudreau N; Xiang H; Xu P; Ni F (Maio de 1999). «Conformation of a Cdc42/Rac interactive binding peptide in complex with Cdc42 and analysis of the binding interface». Biochemistry. 38 (19): 5968–75. PMID 10320322. doi:10.1021/bi990426u 
  23. ↑ a b Abo, A; Qu J; Cammarano M S; Dan C; Fritsch A; Baud V; Belisle B; Minden A (Novembro de 1998). «PAK4, a novel effector for Cdc42Hs, is implicated in the reorganization of the actin cytoskeleton and in the formation of filopodia». EMBO J. 17 (22): 6527–40. PMC 1171000Acessível livremente. 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 (Julho de 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. 275 (29): 21946–52. PMID 10781580. doi:10.1074/jbc.M000687200 
  25. ↑ Miki, H; Sasaki T; Takai Y; Takenawa T (Janeiro de 1998). «Induction of filopodium formation by a WASP-related actin-depolymerizing protein N-WASP». Nature. 391 (6662): 93–6. PMID 9422512. doi:10.1038/34208 
  26. ↑ Gibson, R M; Wilson-Delfosse A L (Outubro de 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. 359 (Pt 2): 285–94. PMC 1222146Acessível livremente. PMID 11583574. doi:10.1042/0264-6021:3590285 
  27. ↑ Hirsch, D S; Pirone D M; Burbelo P D (Janeiro de 2001). «A new family of Cdc42 effector proteins, CEPs, function in fibroblast and epithelial cell shape changes». J. Biol. Chem. 276 (2): 875–83. PMID 11035016. doi:10.1074/jbc.M007039200 
  28. ↑ Low, B C; Seow K T; Guy G R (Maio de 2000). «Evidence for a novel Cdc42GAP domain at the carboxyl terminus of BNIP-2». J. Biol. Chem. 275 (19): 14415–22. PMID 10799524. doi:10.1074/jbc.275.19.14415 
  29. ↑ Low, B C; Seow K T; Guy G R (Dezembro de 2000). «The BNIP-2 and Cdc42GAP homology domain of BNIP-2 mediates its homophilic association and heterophilic interaction with Cdc42GAP». J. Biol. Chem. 275 (48): 37742–51. PMID 10954711. doi:10.1074/jbc.M004897200 
  30. ↑ Qiu, R G; Abo A; Steven Martin G (Junho de 2000). «A human homolog of the C. elegans polarity determinant Par-6 links Rac and Cdc42 to PKCzeta signaling and cell transformation». Curr. Biol. 10 (12): 697–707. 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 (Setembro de 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. 16 (9): 4869–78. PMC 231489Acessível livremente. PMID 8756646. doi:10.1128/MCB.16.9.4869 
  32. ↑ Kuroda, S; Fukata M; Kobayashi K; Nakafuku M; Nomura N; Iwamatsu A; Kaibuchi K (Setembro de 1996). «Identification of IQGAP as a putative target for the small GTPases, Cdc42 and Rac1». J. Biol. Chem. 271 (38): 23363–7. 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 (Junho de 2002). «Rac1 and Cdc42 capture microtubules through IQGAP1 and CLIP-170». Cell. 109 (7): 873–85. PMID 12110184. doi:10.1016/S0092-8674(02)00800-0 
  34. ↑ Hart, M J; Callow M G; Souza B; Polakis P (Junho de 1996). «IQGAP1, a calmodulin-binding protein with a rasGAP-related domain, is a potential effector for cdc42Hs». EMBO J. 15 (12): 2997–3005. PMC 450241Acessível livremente. PMID 8670801. doi:10.1002/j.1460-2075.1996.tb00662.x 
  35. ↑ Joyal, J L; Annan R S; Ho Y D; Huddleston M E; Carr S A; Hart M J; Sacks D B (Junho de 1997). «Calmodulin modulates the interaction between IQGAP1 and Cdc42». J. Biol. Chem. 272 (24): 15419–25. 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 (Outubro de 2001). «Endocytic protein intersectin-l regulates actin assembly via Cdc42 and N-WASP». Nat. Cell Biol. 3 (10): 927–32. 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 (Junho de 2002). «Structural basis for the selective activation of Rho GTPases by Dbl exchange factors». Nat. Struct. Biol. 9 (6): 468–75. PMID 12006984. doi:10.1038/nsb796 
  38. ↑ Aspenström, P (Julho de 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. 7 (7): 479–87. PMID 9210375. doi:10.1016/S0960-9822(06)00219-3 
  39. ↑ a b Tian, L; Nelson D L; Stewart D M (Março de 2000). «Cdc42-interacting protein 4 mediates binding of the Wiskott-Aldrich syndrome protein to microtubules». J. Biol. Chem. 275 (11): 7854–61. PMID 10713100. doi:10.1074/jbc.275.11.7854 
  40. ↑ Böck, B C; Vacratsis P O; Qamirani E; Gallo K A (Maio de 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. 275 (19): 14231–41. PMID 10799501. doi:10.1074/jbc.275.19.14231 
  41. ↑ Soltau, Michaela; Richter Dietmar; Kreienkamp Hans-Jürgen (Dezembro de 2002). «The insulin receptor substrate IRSp53 links postsynaptic shank1 to the small G-protein cdc42». Mol. Cell. Neurosci. 21 (4): 575–83. PMID 12504591. doi:10.1006/mcne.2002.1201 
  42. ↑ Krugmann, S; Jordens I; Gevaert K; Driessens M; Vandekerckhove J; Hall A (Outubro de 2001). «Cdc42 induces filopodia by promoting the formation of an IRSp53:Mena complex». Curr. Biol. 11 (21): 1645–55. PMID 11696321. doi:10.1016/S0960-9822(01)00506-1 
  43. ↑ Miki, H; Yamaguchi H; Suetsugu S; Takenawa T (Dezembro de 2000). «IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling». Nature. 408 (6813): 732–5. PMID 11130076. doi:10.1038/35047107 
  44. ↑ Kim, A S; Kakalis L T; Abdul-Manan N; Liu G A; Rosen M K (Março de 2000). «Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein». Nature. 404 (6774): 151–8. PMID 10724160. doi:10.1038/35004513 
  45. ↑ Kolluri, R; Tolias K F; Carpenter C L; Rosen F S; Kirchhausen T (Maio de 1996). «Direct interaction of the Wiskott-Aldrich syndrome protein with the GTPase Cdc42». Proc. Natl. Acad. Sci. U.S.A. 93 (11): 5615–8. PMC 39296Acessível livremente. 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 (Março de 1996). «Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization». Cell. 84 (5): 723–34. 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 (Julho de 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. 14 (7): 2921–34. PMC 165687Acessível livremente. 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 (Setembro de 2003). «GC-GAP, a Rho family GTPase-activating protein that interacts with signaling adapters Gab1 and Gab2». J. Biol. Chem. 278 (36): 34641–53. PMID 12819203. doi:10.1074/jbc.M304594200 
  49. ↑ Nakamura, Takeshi; Komiya Misako; Sone Kiyoaki; Hirose Eiji; Gotoh Noriko; Morii Hiroshi; Ohta Yasutaka; Mori Nozomu (dezembro de 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». United States. Mol. Cell. Biol. 22 (24): 8721–34. ISSN 0270-7306. PMC 139861Acessível livremente. PMID 12446789. doi:10.1128/MCB.22.24.8721-8734.2002 
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