| Cell division cycle 42 (GTP binding protein, 25kDa) |

PDB rendering based on 1a4r. |
| Available structures |
| PDB |
1A4R, 1AJE, 1AM4, 1AN0, 1CEE, 1CF4, 1DOA, 1E0A, 1EES, 1GRN, 1GZS, 1KI1, 1KZ7, 1KZG, 1NF3, 2ASE, 2DFK, 2KB0, 2NGR, 2ODB, 2QRZ, 2WM9, 2WMN, 2WMO, 3GCG, 3N3V |
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| Identifiers |
| Symbols |
CDC42; CDC42Hs; G25K |
| External IDs |
OMIM: 116952 MGI: 106211 HomoloGene: 124410 GeneCards: CDC42 Gene |
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| RNA expression pattern |
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| More reference expression data |
| Orthologs |
| Species |
Human |
Mouse |
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| Entrez |
998 |
12540 |
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| Ensembl |
ENSG00000070831 |
ENSMUSG00000006699 |
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| UniProt |
P60953 |
Q99JI7 |
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| RefSeq (mRNA) |
NM_001039802.1 |
NM_009861 |
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| RefSeq (protein) |
NP_001034891.1 |
NP_033991 |
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| Location (UCSC) |
Chr 1:
22.38 – 22.42 Mb |
Chr 4:
136.59 – 136.63 Mb |
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| PubMed search |
[1] |
[2] |
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Cell division control protein 42 homolog also known as CDC42 is a protein involved in regulation of the cell cycle. In humans, CDC42 is encoded by the CDC42 gene.[1][2]
[edit] Function
CDC42 is a small GTPase of the Rho-subfamily, which regulates signaling pathways that control diverse cellular functions including cell morphology, migration, endocytosis and cell cycle progression. This protein is highly similar to Saccharomyces cerevisiae Cdc 42, and is able to complement the yeast cdc42-1 mutant. The product of oncogene Dbl was reported to specifically catalyze the dissociation of GDP from this protein. This protein could regulate actin polymerization through its direct binding to Neural Wiskott-Aldrich syndrome protein (N-WASP), which subsequently activates Arp2/3 complex. Alternative splicing of this gene results in multiple transcript variants.[3]
[edit] Interactions
CDC42 has been shown to interact with Phospholipase D1,[4] ARHGAP1,[5][6][7][8] PAK7,[9][10] CDC42EP3,[11][12] PARD6B,[13][14][15] ERRFI1,[16] BNIPL,[17] PAK1,[18][8] ARHGDIA,[19][20] PAK2,[21][22][8] WASL,[23][24] GDI1,[25] CDC42EP2,[26][12] BNIP2,[27][28][7] PARD6A,[14][29][15] IQGAP2,[30] IQGAP1,[31][32][33][34][8] ITSN1,[35][36] TRIP10,[37][38] MAP3K11,[5][39] MAP3K10,[5] BAIAP2,[40][41][42] Wiskott-Aldrich syndrome protein,[38][43][44][45] RICS[46][47][48] and PAK4.[19][9][22]
[edit] References
- ^ 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. doi:10.1073/pnas.87.24.9853. PMC 55272. PMID 2124704. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=55272.
- ^ 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=361395.
- ^ "Entrez Gene: CDC42 cell division cycle 42 (GTP binding protein, 25kDa)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=998.
- ^ 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. doi:10.1074/jbc.M000076200. ISSN 0021-9258. PMID 10747870.
- ^ a b c Nagata, K i; Puls A, Futter C, Aspenstrom P, Schaefer E, Nakata T, Hirokawa N, Hall A (Jan. 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. doi:10.1093/emboj/17.1.149. ISSN 0261-4189. PMC 1170366. PMID 9427749. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1170366.
- ^ Li, R; Zhang B, Zheng Y (Dec. 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. doi:10.1074/jbc.272.52.32830. ISSN 0021-9258. PMID 9407060.
- ^ a b Low, B C; Lim Y P, Lim J, Wong E S, Guy G R (Nov. 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. doi:10.1074/jbc.274.46.33123. ISSN 0021-9258. PMID 10551883.
- ^ a b c d Zhang, B; Chernoff J, Zheng Y (Apr. 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. doi:10.1074/jbc.273.15.8776. ISSN 0021-9258. PMID 9535855.
- ^ a b Dan, Chuntao; Nath Niharika, Liberto Muriel, Minden Audrey (Jan. 2002). "PAK5, a New Brain-Specific Kinase, Promotes Neurite Outgrowth in N1E-115 Cells". Mol. Cell. Biol. (United States) 22 (2): 567–77. doi:10.1128/MCB.22.2.567-577.2002. ISSN 0270-7306. PMC 139731. PMID 11756552. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139731.
- ^ 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. doi:10.1038/sj.onc.1205478. ISSN 0950-9232. PMID 12032833.
- ^ Alberts, A S; Bouquin N, Johnston L H, Treisman R (Apr. 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. doi:10.1074/jbc.273.15.8616. ISSN 0021-9258. PMID 9535835.
- ^ a b Joberty, G; Perlungher R R, Macara I G (Oct. 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=84628.
- ^ Neudauer, C L; Joberty G, Macara I G (Jan. 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. doi:10.1006/bbrc.2000.4160. ISSN 0006-291X. PMID 11162552.
- ^ a b Joberty, G; Petersen C, Gao L, Macara I G (Aug. 2000). "The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42". Nat. Cell Biol. (ENGLAND) 2 (8): 531–9. doi:10.1038/35019573. ISSN 1465-7392. PMID 10934474.
- ^ a b Noda, Y; Takeya R, Ohno S, Naito S, Ito T, Sumimoto H (Feb. 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. doi:10.1046/j.1365-2443.2001.00404.x. ISSN 1356-9597. PMID 11260256.
- ^ Makkinje, A; Quinn D A, Chen A, Cadilla C L, Force T, Bonventre J V, Kyriakis J M (Jun. 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. doi:10.1074/jbc.M909735199. ISSN 0021-9258. PMID 10749885.
- ^ Qin, Wenxin; Hu Jian, Guo Minglei, Xu Jian, Li Jinjun, Yao Genfu, Zhou Xiaomei, Jiang Huiqiu, Zhang Pingping, Shen Li, Wan Dafang, Gu Jianren (Aug. 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. doi:10.1016/S0006-291X(03)01387-1. ISSN 0006-291X. PMID 12901880.
- ^ Seoh, Mui Leng; Ng Chong Han, Yong Jeffery, Lim Louis, Leung Thomas (Mar. 2003). "ArhGAP15, a novel human RacGAP protein with GTPase binding property". FEBS Lett. (Netherlands) 539 (1–3): 131–7. doi:10.1016/S0014-5793(03)00213-8. ISSN 0014-5793. PMID 12650940.
- ^ 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. (England) 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1847948.
- ^ Gorvel, J P; Chang T C, Boretto J, Azuma T, Chavrier P (Jan. 1998). "Differential properties of D4/LyGDI versus RhoGDI: phosphorylation and rho GTPase selectivity". FEBS Lett. (NETHERLANDS) 422 (2): 269–73. doi:10.1016/S0014-5793(98)00020-9. ISSN 0014-5793. PMID 9490022.
- ^ 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. doi:10.1021/bi990426u. ISSN 0006-2960. PMID 10320322.
- ^ a b Abo, A; Qu J, Cammarano M S, Dan C, Fritsch A, Baud V, Belisle B, Minden A (Nov. 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. doi:10.1093/emboj/17.22.6527. ISSN 0261-4189. PMC 1171000. PMID 9822598. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1171000.
- ^ Carlier, M F; Nioche P, Broutin-L'Hermite I, Boujemaa R, Le Clainche C, Egile C, Garbay C, Ducruix A, Sansonetti P, Pantaloni D (Jul. 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. doi:10.1074/jbc.M000687200. ISSN 0021-9258. PMID 10781580.
- ^ Miki, H; Sasaki T, Takai Y, Takenawa T (Jan. 1998). "Induction of filopodium formation by a WASP-related actin-depolymerizing protein N-WASP". Nature (ENGLAND) 391 (6662): 93–6. doi:10.1038/34208. ISSN 0028-0836. PMID 9422512.
- ^ Gibson, R M; Wilson-Delfosse A L (Oct. 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. doi:10.1042/0264-6021:3590285. ISSN 0264-6021. PMC 1222146. PMID 11583574. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1222146.
- ^ Hirsch, D S; Pirone D M, Burbelo P D (Jan. 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. doi:10.1074/jbc.M007039200. ISSN 0021-9258. PMID 11035016.
- ^ 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. doi:10.1074/jbc.275.19.14415. ISSN 0021-9258. PMID 10799524.
- ^ Low, B C; Seow K T, Guy G R (Dec. 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. doi:10.1074/jbc.M004897200. ISSN 0021-9258. PMID 10954711.
- ^ Qiu, R G; Abo A, Steven Martin G (Jun. 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. doi:10.1016/S0960-9822(00)00535-2. ISSN 0960-9822. PMID 10873802.
- ^ Brill, S; Li S, Lyman C W, Church D M, Wasmuth J J, Weissbach L, Bernards A, Snijders A J (Sep. 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=231489.
- ^ Kuroda, S; Fukata M, Kobayashi K, Nakafuku M, Nomura N, Iwamatsu A, Kaibuchi K (Sep. 1996). "Identification of IQGAP as a putative target for the small GTPases, Cdc42 and Rac1". J. Biol. Chem. (UNITED STATES) 271 (38): 23363–7. doi:10.1074/jbc.271.38.23363. ISSN 0021-9258. PMID 8798539.
- ^ Fukata, Masaki; Watanabe Takashi, Noritake Jun, Nakagawa Masato, Yamaga Masaki, Kuroda Shinya, Matsuura Yoshiharu, Iwamatsu Akihiro, Perez Franck, Kaibuchi Kozo (Jun. 2002). "Rac1 and Cdc42 capture microtubules through IQGAP1 and CLIP-170". Cell (United States) 109 (7): 873–85. doi:10.1016/S0092-8674(02)00800-0. ISSN 0092-8674. PMID 12110184.
- ^ Hart, M J; Callow M G, Souza B, Polakis P (Jun. 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=450241.
- ^ Joyal, J L; Annan R S, Ho Y D, Huddleston M E, Carr S A, Hart M J, Sacks D B (Jun. 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. doi:10.1074/jbc.272.24.15419. ISSN 0021-9258. PMID 9182573.
- ^ 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 (Oct. 2001). "Endocytic protein intersectin-l regulates actin assembly via Cdc42 and N-WASP". Nat. Cell Biol. (England) 3 (10): 927–32. doi:10.1038/ncb1001-927. ISSN 1465-7392. PMID 11584276.
- ^ Snyder, Jason T; Worthylake David K, Rossman Kent L, Betts Laurie, Pruitt Wendy M, Siderovski David P, Der Channing J, Sondek John (Jun. 2002). "Structural basis for the selective activation of Rho GTPases by Dbl exchange factors". Nat. Struct. Biol. (United States) 9 (6): 468–75. doi:10.1038/nsb796. ISSN 1072-8368. PMID 12006984.
- ^ Aspenström, P (Jul. 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. doi:10.1016/S0960-9822(06)00219-3. ISSN 0960-9822. PMID 9210375.
- ^ a b Tian, L; Nelson D L, Stewart D M (Mar. 2000). "Cdc42-interacting protein 4 mediates binding of the Wiskott-Aldrich syndrome protein to microtubules". J. Biol. Chem. (UNITED STATES) 275 (11): 7854–61. doi:10.1074/jbc.275.11.7854. ISSN 0021-9258. PMID 10713100.
- ^ 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. doi:10.1074/jbc.275.19.14231. ISSN 0021-9258. PMID 10799501.
- ^ Soltau, Michaela; Richter Dietmar, Kreienkamp Hans-Jürgen (Dec. 2002). "The insulin receptor substrate IRSp53 links postsynaptic shank1 to the small G-protein cdc42". Mol. Cell. Neurosci. (United States) 21 (4): 575–83. doi:10.1006/mcne.2002.1201. ISSN 1044-7431. PMID 12504591.
- ^ Krugmann, S; Jordens I, Gevaert K, Driessens M, Vandekerckhove J, Hall A (Oct. 2001). "Cdc42 induces filopodia by promoting the formation of an IRSp53:Mena complex". Curr. Biol. (England) 11 (21): 1645–55. doi:10.1016/S0960-9822(01)00506-1. ISSN 0960-9822. PMID 11696321.
- ^ Miki, H; Yamaguchi H, Suetsugu S, Takenawa T (Dec. 2000). "IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling". Nature (England) 408 (6813): 732–5. doi:10.1038/35047107. ISSN 0028-0836. PMID 11130076.
- ^ Kim, A S; Kakalis L T, Abdul-Manan N, Liu G A, Rosen M K (Mar. 2000). "Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein". Nature (ENGLAND) 404 (6774): 151–8. doi:10.1038/35004513. ISSN 0028-0836. PMID 10724160.
- ^ 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. doi:10.1073/pnas.93.11.5615. ISSN 0027-8424. PMC 39296. PMID 8643625. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=39296.
- ^ Symons, M; Derry J M, Karlak B, Jiang S, Lemahieu V, Mccormick F, Francke U, Abo A (Mar. 1996). "Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization". Cell (UNITED STATES) 84 (5): 723–34. doi:10.1016/S0092-8674(00)81050-8. ISSN 0092-8674. PMID 8625410.
- ^ Nakazawa, Takanobu; Watabe Ayako M, Tezuka Tohru, Yoshida Yutaka, Yokoyama Kazumasa, Umemori Hisashi, Inoue Akihiro, Okabe Shigeo, Manabe Toshiya, Yamamoto Tadashi (Jul. 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. doi:10.1091/mbc.E02-09-0623. ISSN 1059-1524. PMC 165687. PMID 12857875. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=165687.
- ^ Zhao, Chunmei; Ma Hong, Bossy-Wetzel Ella, Lipton Stuart A, Zhang Zhuohua, Feng Gen-Sheng (Sep. 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. doi:10.1074/jbc.M304594200. ISSN 0021-9258. PMID 12819203.
- ^ Nakamura, Takeshi; Komiya Misako, Sone Kiyoaki, Hirose Eiji, Gotoh Noriko, Morii Hiroshi, Ohta Yasutaka, Mori Nozomu (Dec. 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. doi:10.1128/MCB.22.24.8721-8734.2002. ISSN 0270-7306. PMC 139861. PMID 12446789. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139861.
[edit] Further reading
[edit] External links
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PDB gallery
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1a4r: G12V MUTANT OF HUMAN PLACENTAL CDC42 GTPASE IN THE GDP FORM
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1aje: CDC42 FROM HUMAN, NMR, 20 STRUCTURES
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1am4: COMPLEX BETWEEN CDC42HS.GMPPNP AND P50 RHOGAP (H. SAPIENS)
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1an0: CDC42HS-GDP COMPLEX
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1cee: SOLUTION STRUCTURE OF CDC42 IN COMPLEX WITH THE GTPASE BINDING DOMAIN OF WASP
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1cf4: CDC42/ACK GTPASE-BINDING DOMAIN COMPLEX
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1doa: STRUCTURE OF THE RHO FAMILY GTP-BINDING PROTEIN CDC42 IN COMPLEX WITH THE MULTIFUNCTIONAL REGULATOR RHOGDI
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1e0a: CDC42 COMPLEXED WITH THE GTPASE BINDING DOMAIN OF P21 ACTIVATED KINASE
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1ees: SOLUTION STRUCTURE OF CDC42HS COMPLEXED WITH A PEPTIDE DERIVED FROM P-21 ACTIVATED KINASE, NMR, 20 STRUCTURES
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1grn: CRYSTAL STRUCTURE OF THE CDC42/CDC42GAP/ALF3 COMPLEX.
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1gzs: CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE GEF DOMAIN OF THE SALMONELLA TYPHIMURIUM SOPE TOXIN AND HUMAN CDC42
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1ki1: Guanine Nucleotide Exchange Region of Intersectin in Complex with Cdc42
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1kz7: Crystal Structure of the DH/PH Fragment of Murine Dbs in Complex with the Placental Isoform of Human Cdc42
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1nf3: Structure of Cdc42 in a complex with the GTPase-binding domain of the cell polarity protein, Par6
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2ase: NMR structure of the F28L mutant of Cdc42Hs
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2dfk: Crystal structure of the CDC42-Collybistin II complex
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2ngr: TRANSITION STATE COMPLEX FOR GTP HYDROLYSIS BY CDC42: COMPARISONS OF THE HIGH RESOLUTION STRUCTURES FOR CDC42 BOUND TO THE ACTIVE AND CATALYTICALLY COMPROMISED FORMS OF THE CDC42-GAP.
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2odb: The crystal structure of human cdc42 in complex with the CRIB domain of human p21-activated kinase 6 (PAK6)
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| 3.6.1 |
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| 3.6.2 |
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| 3.6.3-4: ATPase |
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| 3.6.5: GTPase |
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Rho family of GTPases: Cdc42 (CDC42, TC10, TCL) • RhoUV (RhoU, RhoV) • Rac (Rac1, 2, 3, RhoG) • RhoBTB (1, 2) • RhoH • Rho (A, B, C) • Rnd (1, 2, 3) • RhoDF (RhoF, RhoD)
other: Ras ( HRAS, KRAS, NRAS) · Rab ( RAB23, RAB27) · Arf ( ARF6, SAR1B, ARL13B, ARL6) · Ran · Rheb · Rap
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| Cyclin |
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| CDK |
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| CDK inhibitor |
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| P53 p63 p73 family |
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Phases and
checkpoints |
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B bsyn: dna (repl, cycl, reco, repr) · tscr (fact, tcrg, nucl, rnat, rept, ptts) · tltn (risu, pttl, nexn) · dnab, rnab/runp · stru (domn, 1°, 2°, 3°, 4°)
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| 3.6.1 |
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| 3.6.2 |
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| 3.6.3-4: ATPase |
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| 3.6.5: GTPase |
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Rho family of GTPases: Cdc42 (CDC42, TC10, TCL) • RhoUV (RhoU, RhoV) • Rac (Rac1, 2, 3, RhoG) • RhoBTB (1, 2) • RhoH • Rho (A, B, C) • Rnd (1, 2, 3) • RhoDF (RhoF, RhoD)
other: Ras ( HRAS, KRAS, NRAS) · Rab ( RAB23, RAB27) · Arf ( ARF6, SAR1B, ARL13B, ARL6) · Ran · Rheb · Rap
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