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词条 CDC42
释义

  1. Function

  2. Structure

  3. Role in cancer

  4. Interactions

  5. References

  6. External links

Cell division control protein 42 homolog, also known as Cdc42, is a protein involved in regulation of the cell cycle. It was originally identified in S. cerevisiae (yeast) as a mediator of cell division, and is now known to influence a variety of signaling events and cellular processes in a variety of organisms from yeast to mammals.{{Infobox_gene}}

Function

Human Cdc42 is a small GTPase of the Rho family, which regulates signaling pathways that control diverse cellular functions including cell morphology, cell migration, endocytosis and cell cycle progression.[1] Rho GTPases are central to dynamic actin cytoskeletal assembly and rearrangement that are the basis of cell-cell adhesion and migration. Activated Cdc42 activates by conformational changes[2] p21-activated kinases PAK1 and PAK2, which in turn initiate actin reorganization and regulate cell adhesion, migration, and invasion.[3]

Structure

Cdc42 is a homodimer with A and B chains.[4] Its total length is 191 amino acids and its theoretical weight is 21.33 KDa.[4] Its sequence domains include a P-loop containing nucleoside triphosphate hydrolase and a small GTP-binding protein domain.[4]

Cdc42 cycles between an active GTP-bound state and an inactive GDP-bound state. This process is regulated by guanine nucleotide exchange factors (GEFs) which promote the exchange of bound GDP for free GTP, GTPase activating proteins (GAPs) which increase GTP hydrolysis activity, and GDP dissociation inhibitors which inhibit the dissociation of the nucleotide from the GTPase.[5]

Role in cancer

Recently, Cdc42 has been shown to actively assist in cancer progression. Several studies have established the basis for this and hypothesized about the underlying mechanisms.

Cdc42 is overexpressed in non-small cell lung cancer, colorectal adenocarcinoma, melanoma, breast cancer, and testicular cancer.[6] Elevated levels of the protein have been correlated with negative patient survival. Cdc42 has also been shown to be required for both G1-S phase progression and mitosis, and it also modulates the transcription factors SRF, STAT3, and NFkB.[6] It has been hypothesized that targeting Cdc42 in conjunction with chemotherapy may be an effective cancer treatment strategy.

In one study studying the role of Cdc42 in cervical cancer, immunohistochemistry was used to detect Cdc42 expression in three types of tissues: normal cervical tissues, cervical intraepithelial neoplasia (CIN) I or below, CIN II or above, and cervical cancer tissues.[7] Cdc42 expression was gradually increased showing significant difference and was significantly higher in HeLa cells than in regular cells. The migration ability of HeLa cells transfected with Cdc42 was higher than that of non-transfected cells.[7] It was proposed that the overexpression of Cdc42 can promote filopodia formation in HeLa cells. Cdc42 overexpression significantly improved the ability of cervical cancer cells to migrate, possibly due to improved pseudopodia formation.[7]

Another study found that Cdc42 drives the process of initiating a metastatic tumor in a new tissue by promoting the expression of β1 integrin, an adhesion receptor known to be involved in metastasis.[8] Levels of β1 integrin were reduced in Cdc42-deficient cells. β1 integrin is important for adhesion to the extracellular matrix, and could be important for the initial attachment to endothelial cells as well. Knocking down β1 integrin inhibited cancer cell migration, whereas overexpressing the integrin in Cdc42-deficient cells restored endothelial invasion.[8] Cdc42 promoted β1 integrin expression by activating a transcription factor called SRF. A continually active form of the transcription factor was also capable of restoring endothelial insertion to cancer cells lacking Cdc42.

Normal cancer cells and Cdc42-deficient cancer cells have also been compared in vivo. When both types of cells were injected into mouse tail veins, control cells spread out more on the vessel endothelium within minutes, suggesting that Cdc42 assists in cell migration.[8] After six weeks, the control cells had generated more metastases than the Cdc42-deficient cells. Invading cancer cells send out protrusions that reach down between neighboring endothelial cells to contact the underlying basement membrane. The cancer cells then spread out on this extracellular matrix so that the endothelial cells retract, and allow the invaders to insert themselves between them.[8] In the absence of Cdc42, cancer cells failed to spread out on the basement membrane, and Cdc42-deficient cells showed reduced adhesion to extracellular matrix-coated coverslips.[8] Cdc42 therefore promotes the attachment of cancer cells to both endothelial cells and the underlying basement membrane during transendothelial migration.

The small molecular inhibitor AZA197 has been used to inhibit Cdc42 in the treatment of KRAS mutant colorectal cancers.[9] There was evidence that Cdc42 inhibition by AZA197 treatment suppresses proliferative and pro-survival signaling pathways via PAK1-ERK signaling and reduces colon cancer cell migration and invasion.[9] In mice, systemic AZA197 treatment in vivo reduced primary tumor growth and prolonged survival.[9] Therapy targeting Rho GTPase Cdc42 signaling pathways may be effective for treatment of patients with advanced colon cancer overexpressing Cdc42, and particularly those with KRAS-mutant disease.

Interactions

CDC42 has been shown to interact with:

{{div col|colwidth=20em}}
  • ARHGAP1,[10][11][12][13]
  • ARHGDIA,[14][15]
  • BAIAP2,[16][17][18]
  • BNIP2,[12][19][20]
  • BNIPL,[21]
  • CDC42EP2,[34][22]
  • CDC42EP3,[23][24]
  • ERRFI1,[25]
  • GDI1,[26]
  • IQGAP1,[13][27][28][29][30]
  • IQGAP2,[31]
  • ITSN1,[32][33]
  • MAP3K10,[10]
  • MAP3K11,[10][34]
  • PAK1,[13][35]
  • PAK2,[13][36][37]
  • PAK4.[14][37][58]
  • PAK7,[38][39]
  • PARD6A,[61][62][40]
  • PARD6B,[41][42][43]
  • Phospholipase D1,[44]
  • RICS[45][46][47]
  • TRIP10,[48][49]
  • WASL,[50][51]
  • Wiskott-Aldrich syndrome protein,[49][52][53][54]
{{Div col end}}

References

1. ^{{cite journal | vauthors = Qadir MI, Parveen A, Ali M | title = Cdc42: Role in Cancer Management | journal = Chemical Biology & Drug Design | volume = 86 | issue = 4 | pages = 432–9 | date = October 2015 | pmid = 25777055 | doi = 10.1111/cbdd.12556 }}
2. ^{{cite journal | vauthors = Bishop AL, Hall A | title = Rho GTPases and their effector proteins | journal = The Biochemical Journal | volume = 348 | issue = 2 | pages = 241–255 | date = June 2000 | pmid = 10816416 | pmc = 1221060 | doi = 10.1042/bj3480241 }}
3. ^{{cite journal | vauthors = Guo Y, Kenney SR, Muller CY, Adams S, Rutledge T, Romero E, Murray-Krezan C, Prekeris R, Sklar LA, Hudson LG, Wandinger-Ness A | title = R-Ketorolac Targets Cdc42 and Rac1 and Alters Ovarian Cancer Cell Behaviors Critical for Invasion and Metastasis | journal = Molecular Cancer Therapeutics | volume = 14 | issue = 10 | pages = 2215–27 | date = October 2015 | pmid = 26206334 | pmc = 4596774 | doi = 10.1158/1535-7163.MCT-15-0419 }}
4. ^1 2 {{cite web | url = https://www.ebi.ac.uk/pdbe/entry/pdb/1a4r | title = PDB 1a4r structure summary | publisher = EMBL-EBI | work = Protein Data Bank in Europe | access-date = 2016-04-22 }}
5. ^{{cite web | url = http://atlasgeneticsoncology.org/Genes/GC_CDC42.html | title = CDC42 (cell division cycle 42 (GTP binding protein, 25kDa)) | website = atlasgeneticsoncology.org | access-date = 2016-04-22 }}
6. ^1 {{cite journal | vauthors = Stengel K, Zheng Y | title = Cdc42 in oncogenic transformation, invasion, and tumorigenesis | journal = Cellular Signalling | volume = 23 | issue = 9 | pages = 1415–23 | date = September 2011 | pmid = 21515363 | pmc = 3115433 | doi = 10.1016/j.cellsig.2011.04.001 }}
7. ^1 2 {{cite journal | vauthors = Ye H, Zhang Y, Geng L, Li Z | title = Cdc42 expression in cervical cancer and its effects on cervical tumor invasion and migration | journal = International Journal of Oncology | volume = 46 | issue = 2 | pages = 757–63 | date = February 2015 | pmid = 25394485 | doi = 10.3892/ijo.2014.2748 }}
8. ^1 2 3 4 {{cite journal | vauthors = Wilson JM, Menkhaus P, Gustin BW | title = Volume and outcome of coronary artery bypass graft surgery | journal = JAMA | volume = 257 | issue = 18 | pages = 2434–5 | date = May 1987 | pmc = 3494856 | doi = 10.1083/jcb.1994if | pmid = 3494856 | url = http://jcb.rupress.org/content/199/4/567 }}
9. ^1 2 {{cite journal | vauthors = Zins K, Gunawardhana S, Lucas T, Abraham D, Aharinejad S | title = Targeting Cdc42 with the small molecule drug AZA197 suppresses primary colon cancer growth and prolongs survival in a preclinical mouse xenograft model by downregulation of PAK1 activity | journal = Journal of Translational Medicine | volume = 11 | pages = 295 | date = 2013-01-01 | pmid = 24279335 | pmc = 4222769 | doi = 10.1186/1479-5876-11-295 }}
10. ^1 2 {{cite journal | vauthors = Nagata K, Puls A, Futter C, Aspenstrom P, Schaefer E, Nakata T, Hirokawa N, Hall A | title = The MAP kinase kinase kinase MLK2 co-localizes with activated JNK along microtubules and associates with kinesin superfamily motor KIF3 | journal = The EMBO Journal | volume = 17 | issue = 1 | pages = 149–58 | date = January 1998 | pmid = 9427749 | pmc = 1170366 | doi = 10.1093/emboj/17.1.149 }}
11. ^{{cite journal | vauthors = Li R, Zhang B, Zheng Y | title = Structural determinants required for the interaction between Rho GTPase and the GTPase-activating domain of p190 | journal = The Journal of Biological Chemistry | volume = 272 | issue = 52 | pages = 32830–5 | date = December 1997 | pmid = 9407060 | doi = 10.1074/jbc.272.52.32830 }}
12. ^1 {{cite journal | vauthors = Low BC, Lim YP, Lim J, Wong ES, Guy GR | title = Tyrosine phosphorylation of the Bcl-2-associated protein BNIP-2 by fibroblast growth factor receptor-1 prevents its binding to Cdc42GAP and Cdc42 | journal = The Journal of Biological Chemistry | volume = 274 | issue = 46 | pages = 33123–30 | date = November 1999 | pmid = 10551883 | doi = 10.1074/jbc.274.46.33123 }}
13. ^1 2 3 {{cite journal | vauthors = Zhang B, Chernoff J, Zheng Y | title = Interaction of Rac1 with GTPase-activating proteins and putative effectors. A comparison with Cdc42 and RhoA | journal = The Journal of Biological Chemistry | volume = 273 | issue = 15 | pages = 8776–82 | date = April 1998 | pmid = 9535855 | doi = 10.1074/jbc.273.15.8776 }}
14. ^1 {{cite journal | vauthors = Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D | title = Large-scale mapping of human protein-protein interactions by mass spectrometry | journal = Molecular Systems Biology | volume = 3 | issue = 1 | pages = 89 | year = 2007 | pmid = 17353931 | pmc = 1847948 | doi = 10.1038/msb4100134 }}
15. ^{{cite journal | vauthors = Gorvel JP, Chang TC, Boretto J, Azuma T, Chavrier P | title = Differential properties of D4/LyGDI versus RhoGDI: phosphorylation and rho GTPase selectivity | journal = FEBS Letters | volume = 422 | issue = 2 | pages = 269–73 | date = January 1998 | pmid = 9490022 | doi = 10.1016/S0014-5793(98)00020-9 }}
16. ^{{cite journal | vauthors = Soltau M, Richter D, Kreienkamp HJ | title = The insulin receptor substrate IRSp53 links postsynaptic shank1 to the small G-protein cdc42 | journal = Molecular and Cellular Neurosciences | volume = 21 | issue = 4 | pages = 575–83 | date = December 2002 | pmid = 12504591 | doi = 10.1006/mcne.2002.1201 }}
17. ^{{cite journal | vauthors = Krugmann S, Jordens I, Gevaert K, Driessens M, Vandekerckhove J, Hall A | title = Cdc42 induces filopodia by promoting the formation of an IRSp53:Mena complex | journal = Current Biology | volume = 11 | issue = 21 | pages = 1645–55 | date = October 2001 | pmid = 11696321 | doi = 10.1016/S0960-9822(01)00506-1 }}
18. ^{{cite journal | vauthors = Miki H, Yamaguchi H, Suetsugu S, Takenawa T | title = IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling | journal = Nature | volume = 408 | issue = 6813 | pages = 732–5 | date = December 2000 | pmid = 11130076 | doi = 10.1038/35047107 }}
19. ^{{cite journal | vauthors = Low BC, Seow KT, Guy GR | title = Evidence for a novel Cdc42GAP domain at the carboxyl terminus of BNIP-2 | journal = The Journal of Biological Chemistry | volume = 275 | issue = 19 | pages = 14415–22 | date = May 2000 | pmid = 10799524 | doi = 10.1074/jbc.275.19.14415 }}
20. ^{{cite journal | vauthors = Low BC, Seow KT, Guy GR | title = The BNIP-2 and Cdc42GAP homology domain of BNIP-2 mediates its homophilic association and heterophilic interaction with Cdc42GAP | journal = The Journal of Biological Chemistry | volume = 275 | issue = 48 | pages = 37742–51 | date = December 2000 | pmid = 10954711 | doi = 10.1074/jbc.M004897200 }}
21. ^{{cite journal | vauthors = Qin W, Hu J, Guo M, Xu J, Li J, Yao G, Zhou X, Jiang H, Zhang P, Shen L, Wan D, Gu J | title = BNIPL-2, a novel homologue of BNIP-2, interacts with Bcl-2 and Cdc42GAP in apoptosis | journal = Biochemical and Biophysical Research Communications | volume = 308 | issue = 2 | pages = 379–85 | date = August 2003 | pmid = 12901880 | doi = 10.1016/S0006-291X(03)01387-1 }}
22. ^{{cite journal | vauthors = Hirsch DS, Pirone DM, Burbelo PD | title = A new family of Cdc42 effector proteins, CEPs, function in fibroblast and epithelial cell shape changes | journal = The Journal of Biological Chemistry | volume = 276 | issue = 2 | pages = 875–83 | date = January 2001 | pmid = 11035016 | doi = 10.1074/jbc.M007039200 }}
23. ^1 {{cite journal | vauthors = Joberty G, Perlungher RR, Macara IG | title = The Borgs, a new family of Cdc42 and TC10 GTPase-interacting proteins | journal = Molecular and Cellular Biology | volume = 19 | issue = 10 | pages = 6585–97 | date = October 1999 | pmid = 10490598 | pmc = 84628 | doi = 10.1128/MCB.19.10.6585 }}
24. ^{{cite journal | vauthors = Alberts AS, Bouquin N, Johnston LH, Treisman R | title = Analysis of RhoA-binding proteins reveals an interaction domain conserved in heterotrimeric G protein beta subunits and the yeast response regulator protein Skn7 | journal = The Journal of Biological Chemistry | volume = 273 | issue = 15 | pages = 8616–22 | date = April 1998 | pmid = 9535835 | doi = 10.1074/jbc.273.15.8616 }}
25. ^{{cite journal | vauthors = Makkinje A, Quinn DA, Chen A, Cadilla CL, Force T, Bonventre JV, Kyriakis JM | title = 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 | journal = The Journal of Biological Chemistry | volume = 275 | issue = 23 | pages = 17838–47 | date = June 2000 | pmid = 10749885 | doi = 10.1074/jbc.M909735199 | pmc = 3668664 }}
26. ^{{cite journal | vauthors = Gibson RM, Wilson-Delfosse AL | title = RhoGDI-binding-defective mutant of Cdc42Hs targets to membranes and activates filopodia formation but does not cycle with the cytosol of mammalian cells | journal = The Biochemical Journal | volume = 359 | issue = Pt 2 | pages = 285–94 | date = October 2001 | pmid = 11583574 | pmc = 1222146 | doi = 10.1042/0264-6021:3590285 }}
27. ^{{cite journal | vauthors = Kuroda S, Fukata M, Kobayashi K, Nakafuku M, Nomura N, Iwamatsu A, Kaibuchi K | title = Identification of IQGAP as a putative target for the small GTPases, Cdc42 and Rac1 | journal = The Journal of Biological Chemistry | volume = 271 | issue = 38 | pages = 23363–7 | date = September 1996 | pmid = 8798539 | doi = 10.1074/jbc.271.38.23363 }}
28. ^{{cite journal | vauthors = Fukata M, Watanabe T, Noritake J, Nakagawa M, Yamaga M, Kuroda S, Matsuura Y, Iwamatsu A, Perez F, Kaibuchi K | title = Rac1 and Cdc42 capture microtubules through IQGAP1 and CLIP-170 | journal = Cell | volume = 109 | issue = 7 | pages = 873–85 | date = June 2002 | pmid = 12110184 | doi = 10.1016/S0092-8674(02)00800-0 }}
29. ^{{cite journal | vauthors = Hart MJ, Callow MG, Souza B, Polakis P | title = IQGAP1, a calmodulin-binding protein with a rasGAP-related domain, is a potential effector for cdc42Hs | journal = The EMBO Journal | volume = 15 | issue = 12 | pages = 2997–3005 | date = June 1996 | pmid = 8670801 | pmc = 450241 | doi = 10.1002/j.1460-2075.1996.tb00663.x }}
30. ^{{cite journal | vauthors = Joyal JL, Annan RS, Ho YD, Huddleston ME, Carr SA, Hart MJ, Sacks DB | title = Calmodulin modulates the interaction between IQGAP1 and Cdc42. Identification of IQGAP1 by nanoelectrospray tandem mass spectrometry | journal = The Journal of Biological Chemistry | volume = 272 | issue = 24 | pages = 15419–25 | date = June 1997 | pmid = 9182573 | doi = 10.1074/jbc.272.24.15419 }}
31. ^{{cite journal | vauthors = Brill S, Li S, Lyman CW, Church DM, Wasmuth JJ, Weissbach L, Bernards A, Snijders AJ | title = The Ras GTPase-activating-protein-related human protein IQGAP2 harbors a potential actin binding domain and interacts with calmodulin and Rho family GTPases | journal = Molecular and Cellular Biology | volume = 16 | issue = 9 | pages = 4869–78 | date = September 1996 | pmid = 8756646 | pmc = 231489 | doi = 10.1128/mcb.16.9.4869 }}
32. ^{{cite journal | vauthors = Hussain NK, Jenna S, Glogauer M, Quinn CC, Wasiak S, Guipponi M, Antonarakis SE, Kay BK, Stossel TP, Lamarche-Vane N, McPherson PS | title = Endocytic protein intersectin-l regulates actin assembly via Cdc42 and N-WASP | journal = Nature Cell Biology | volume = 3 | issue = 10 | pages = 927–32 | date = October 2001 | pmid = 11584276 | doi = 10.1038/ncb1001-927 }}
33. ^{{cite journal | vauthors = Snyder JT, Worthylake DK, Rossman KL, Betts L, Pruitt WM, Siderovski DP, Der CJ, Sondek J | title = Structural basis for the selective activation of Rho GTPases by Dbl exchange factors | journal = Nature Structural Biology | volume = 9 | issue = 6 | pages = 468–75 | date = June 2002 | pmid = 12006984 | doi = 10.1038/nsb796 }}
34. ^{{cite journal | vauthors = Böck BC, Vacratsis PO, Qamirani E, Gallo KA | title = Cdc42-induced activation of the mixed-lineage kinase SPRK in vivo. Requirement of the Cdc42/Rac interactive binding motif and changes in phosphorylation | journal = The Journal of Biological Chemistry | volume = 275 | issue = 19 | pages = 14231–41 | date = May 2000 | pmid = 10799501 | doi = 10.1074/jbc.275.19.14231 }}
35. ^{{cite journal | vauthors = Seoh ML, Ng CH, Yong J, Lim L, Leung T | title = ArhGAP15, a novel human RacGAP protein with GTPase binding property | journal = FEBS Letters | volume = 539 | issue = 1–3 | pages = 131–7 | date = March 2003 | pmid = 12650940 | doi = 10.1016/S0014-5793(03)00213-8 }}
36. ^{{cite journal | vauthors = Stevens WK, Vranken W, Goudreau N, Xiang H, Xu P, Ni F | title = Conformation of a Cdc42/Rac interactive binding peptide in complex with Cdc42 and analysis of the binding interface | journal = Biochemistry | volume = 38 | issue = 19 | pages = 5968–75 | date = May 1999 | pmid = 10320322 | doi = 10.1021/bi990426u }}
37. ^1 {{cite journal | vauthors = Abo A, Qu J, Cammarano MS, Dan C, Fritsch A, Baud V, Belisle B, Minden A | title = PAK4, a novel effector for Cdc42Hs, is implicated in the reorganization of the actin cytoskeleton and in the formation of filopodia | journal = The EMBO Journal | volume = 17 | issue = 22 | pages = 6527–40 | date = November 1998 | pmid = 9822598 | pmc = 1171000 | doi = 10.1093/emboj/17.22.6527 }}
38. ^1 {{cite journal | vauthors = Dan C, Nath N, Liberto M, Minden A | title = PAK5, a new brain-specific kinase, promotes neurite outgrowth in N1E-115 cells | journal = Molecular and Cellular Biology | volume = 22 | issue = 2 | pages = 567–77 | date = January 2002 | pmid = 11756552 | pmc = 139731 | doi = 10.1128/MCB.22.2.567-577.2002 }}
39. ^{{cite journal | vauthors = Pandey A, Dan I, Kristiansen TZ, Watanabe NM, Voldby J, Kajikawa E, Khosravi-Far R, Blagoev B, Mann M | title = Cloning and characterization of PAK5, a novel member of mammalian p21-activated kinase-II subfamily that is predominantly expressed in brain | journal = Oncogene | volume = 21 | issue = 24 | pages = 3939–48 | date = May 2002 | pmid = 12032833 | doi = 10.1038/sj.onc.1205478 }}
40. ^{{cite journal | vauthors = Qiu RG, Abo A, Steven Martin G | title = A human homolog of the C. elegans polarity determinant Par-6 links Rac and Cdc42 to PKCzeta signaling and cell transformation | journal = Current Biology | volume = 10 | issue = 12 | pages = 697–707 | date = June 2000 | pmid = 10873802 | doi = 10.1016/S0960-9822(00)00535-2 }}
41. ^1 {{cite journal | vauthors = Joberty G, Petersen C, Gao L, Macara IG | title = The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42 | journal = Nature Cell Biology | volume = 2 | issue = 8 | pages = 531–9 | date = August 2000 | pmid = 10934474 | doi = 10.1038/35019573 }}
42. ^1 {{cite journal | vauthors = Noda Y, Takeya R, Ohno S, Naito S, Ito T, Sumimoto H | title = 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 | journal = Genes to Cells | volume = 6 | issue = 2 | pages = 107–19 | date = February 2001 | pmid = 11260256 | doi = 10.1046/j.1365-2443.2001.00404.x }}
43. ^{{cite journal | vauthors = Neudauer CL, Joberty G, Macara IG | title = PIST: a novel PDZ/coiled-coil domain binding partner for the rho-family GTPase TC10 | journal = Biochemical and Biophysical Research Communications | volume = 280 | issue = 2 | pages = 541–7 | date = January 2001 | pmid = 11162552 | doi = 10.1006/bbrc.2000.4160 }}
44. ^{{cite journal | vauthors = Walker SJ, Wu WJ, Cerione RA, Brown HA | title = Activation of phospholipase D1 by Cdc42 requires the Rho insert region | journal = The Journal of Biological Chemistry | volume = 275 | issue = 21 | pages = 15665–8 | date = May 2000 | pmid = 10747870 | doi = 10.1074/jbc.M000076200 }}
45. ^{{cite journal | vauthors = Nakazawa T, Watabe AM, Tezuka T, Yoshida Y, Yokoyama K, Umemori H, Inoue A, Okabe S, Manabe T, Yamamoto T | title = p250GAP, a novel brain-enriched GTPase-activating protein for Rho family GTPases, is involved in the N-methyl-d-aspartate receptor signaling | journal = Molecular Biology of the Cell | volume = 14 | issue = 7 | pages = 2921–34 | date = July 2003 | pmid = 12857875 | pmc = 165687 | doi = 10.1091/mbc.E02-09-0623 }}
46. ^{{cite journal | vauthors = Zhao C, Ma H, Bossy-Wetzel E, Lipton SA, Zhang Z, Feng GS | title = GC-GAP, a Rho family GTPase-activating protein that interacts with signaling adapters Gab1 and Gab2 | journal = The Journal of Biological Chemistry | volume = 278 | issue = 36 | pages = 34641–53 | date = September 2003 | pmid = 12819203 | doi = 10.1074/jbc.M304594200 }}
47. ^{{cite journal | vauthors = Nakamura T, Komiya M, Sone K, Hirose E, Gotoh N, Morii H, Ohta Y, Mori N | title = 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 | journal = Molecular and Cellular Biology | volume = 22 | issue = 24 | pages = 8721–34 | date = December 2002 | pmid = 12446789 | pmc = 139861 | doi = 10.1128/MCB.22.24.8721-8734.2002 }}
48. ^{{cite journal | vauthors = Aspenström P | title = A Cdc42 target protein with homology to the non-kinase domain of FER has a potential role in regulating the actin cytoskeleton | journal = Current Biology | volume = 7 | issue = 7 | pages = 479–87 | date = July 1997 | pmid = 9210375 | doi = 10.1016/S0960-9822(06)00219-3 }}
49. ^1 {{cite journal | vauthors = Tian L, Nelson DL, Stewart DM | title = Cdc42-interacting protein 4 mediates binding of the Wiskott-Aldrich syndrome protein to microtubules | journal = The Journal of Biological Chemistry | volume = 275 | issue = 11 | pages = 7854–61 | date = March 2000 | pmid = 10713100 | doi = 10.1074/jbc.275.11.7854 }}
50. ^{{cite journal | vauthors = Carlier MF, Nioche P, Broutin-L'Hermite I, Boujemaa R, Le Clainche C, Egile C, Garbay C, Ducruix A, Sansonetti P, Pantaloni D | title = GRB2 links signaling to actin assembly by enhancing interaction of neural Wiskott-Aldrich syndrome protein (N-WASp) with actin-related protein (ARP2/3) complex | journal = The Journal of Biological Chemistry | volume = 275 | issue = 29 | pages = 21946–52 | date = July 2000 | pmid = 10781580 | doi = 10.1074/jbc.M000687200 }}
51. ^{{cite journal | vauthors = Miki H, Sasaki T, Takai Y, Takenawa T | title = Induction of filopodium formation by a WASP-related actin-depolymerizing protein N-WASP | journal = Nature | volume = 391 | issue = 6662 | pages = 93–6 | date = January 1998 | pmid = 9422512 | doi = 10.1038/34208 }}
52. ^{{cite journal | vauthors = Kim AS, Kakalis LT, Abdul-Manan N, Liu GA, Rosen MK | title = Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein | journal = Nature | volume = 404 | issue = 6774 | pages = 151–8 | date = March 2000 | pmid = 10724160 | doi = 10.1038/35004513 }}
53. ^{{cite journal | vauthors = Kolluri R, Tolias KF, Carpenter CL, Rosen FS, Kirchhausen T | title = Direct interaction of the Wiskott-Aldrich syndrome protein with the GTPase Cdc42 | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 93 | issue = 11 | pages = 5615–8 | date = May 1996 | pmid = 8643625 | pmc = 39296 | doi = 10.1073/pnas.93.11.5615 }}
54. ^{{cite journal | vauthors = Symons M, Derry JM, Karlak B, Jiang S, Lemahieu V, Mccormick F, Francke U, Abo A | title = Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization | journal = Cell | volume = 84 | issue = 5 | pages = 723–34 | date = March 1996 | pmid = 8625410 | doi = 10.1016/S0092-8674(00)81050-8 }}

External links

{{Commons category|CDC42}}
  • {{MeshName|cdc42+GTP-Binding+Protein}}
  • CDC42 Info with links in the Cell Migration Gateway
  • {{UCSC gene info|CDC42}}
{{PDB Gallery|geneid=998}}{{GTPases}}{{Cell cycle proteins}}{{Rho family of GTPases}}
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