Targeting Cdc42 in cancer

Bibliography

• Colicelli J. Human RAS superfamily proteins and related GTPases. Sci STKE 2004;2004(250):RE13
   PubMedGoogle Scholar
• Sahai E, Marshall CJ. RHO-GTPases and cancer. Nat Rev Cancer 2002;2(2):133-42
   PubMed Web of Science ®Google Scholar
• Tang Y, Olufemi L, Wang MT, Nie D. Role of Rho GTPases in breast cancer. Front Biosci 2008;13:759-76
   PubMed Web of Science ®Google Scholar
• Melendez J, Grogg M, Zheng Y. Signaling role of Cdc42 in regulating mammalian physiology. J Biol Chem 2011;286(4):2375-81
   PubMed Web of Science ®Google Scholar
• Ridley AJ. Rho family proteins: coordinating cell responses. Trends Cell Biol 2001;11(12):471-7
   Google Scholar
• Cherfils J, Chardin P. GEFs: structural basis for their activation of small GTP-binding proteins. Trends Biochem Sci 1999;24(8):306-11
   PubMed Web of Science ®Google Scholar
• Riou P, Kjaer S, Garg R, et al. 14-3-3 proteins interact with a hybrid prenyl-phosphorylation motif to inhibit g proteins. Cell 2013;153(3):640-53
   PubMed Web of Science ®Google Scholar
• Johnson DI, Pringle JR. Molecular characterization of CDC42, a Saccharomyces cerevisiae gene involved in the development of cell polarity. J Cell Biol 1990;111(1):143-52
   PubMed Web of Science ®Google Scholar
• Gotta M, Abraham MC, Ahringer J. CDC-42 controls early cell polarity and spindle orientation in C. elegans. Curr Biol 2001;11(7):482-8
   PubMed Web of Science ®Google Scholar
• Murphy AM, Montell DJ. Cell type-specific roles for Cdc42, Rac, and RhoL in Drosophila oogenesis. J Cell Biol 1996;133(3):617-30
   Google Scholar
• Wang L, Zheng Y. Cell type-specific functions of Rho GTPases revealed by gene targeting in mice. Trends Cell Biol 2007;17(2):58-64
   Google Scholar
• Chen F, Ma L, Parrini MC, et al. Cdc42 is required for PIP(2)-induced actin polymerization and early development but not for cell viability. Curr Biol 2000;10(13):758-65
   Google Scholar
• Martin-Belmonte F, Gassama A, Datta A, et al. PTEN-mediated apical segregation of phosphoinositides controls epithelial morphogenesis through Cdc42. Cell 2007;128(2):383-97
   Google Scholar
• Kesavan G, Sand FW, Greiner TU, et al. Cdc42-mediated tubulogenesis controls cell specification. Cell 2009;139(4):791-801
   Google Scholar
• Cappello S, Attardo A, Wu X, et al. The Rho-GTPase cdc42 regulates neural progenitor fate at the apical surface. Nat Neurosci 2006;9(9):1099-107
   Google Scholar
• van Hengel J, D'Hooge P, Hooghe B, et al. Continuous cell injury promotes hepatic tumorigenesis in cdc42-deficient mouse liver. Gastroenterology 2008;134(3):781-92
   Google Scholar
• Guo F, Velu CS, Grimes HL, Zheng Y. Rho GTPase Cdc42 is essential for B-lymphocyte development and activation. Blood 2009;114(14):2909-16
   Google Scholar
• Ito Y, Teitelbaum SL, Zou W, et al. Cdc42 regulates bone modeling and remodeling in mice by modulating RANKL/M-CSF signaling and osteoclast polarization. J Clin Investigat 2010;120(6):1981-93
   PubMed Web of Science ®Google Scholar
• Schubbert S, Shannon K, Bollag G. Hyperactive Ras in developmental disorders and cancer. Nat Rev Cancer 2007;7(4):295-308
   PubMed Web of Science ®Google Scholar
• Qiu RG, Abo A, McCormick F, Symons M. Cdc42 regulates anchorage-independent growth and is necessary for Ras transformation. Mol Cell Biol 1997;17(6):3449-58
   PubMedGoogle Scholar
• Bagrodia S, Laudano AP, Shalloway D. Accessibility of the c-Src SH2-domain for binding is increased during mitosis. J Biol Chem 1994;269(14):10247-51
   Google Scholar
• Beeser A, Jaffer ZM, Hofmann C, Chernoff J. Role of group A p21-activated kinases in activation of extracellular-regulated kinase by growth factors. J Biol Chem 2005;280(44):36609-15
   PubMed Web of Science ®Google Scholar
• Stengel KR, Zheng Y. Essential role of Cdc42 in Ras-induced transformation revealed by gene targeting. PLoS One 2012;7(6):e37317
   Google Scholar
• Wu WJ, Tu S, Cerione RA. Activated Cdc42 sequesters c-Cbl and prevents EGF receptor degradation. Cell 2003;114(6):715-25
   Google Scholar
• Cerione RA. Cdc42: new roads to travel. Trends Cell Biol 2004;14(3):127-32
   Google Scholar
• Hirsch DS, Shen Y, Wu WJ. Growth and motility inhibition of breast cancer cells by epidermal growth factor receptor degradation is correlated with inactivation of Cdc42. Cancer Res 2006;66(7):3523-30
   Google Scholar
• Rihet S, Vielh P, Camonis J, et al. Mutation status of genes encoding RhoA, Rac1, and Cdc42 GTPases in a panel of invasive human colorectal and breast tumors. J Cancer Res Clin Oncol 2001;127(12):733-8
   Google Scholar
• Nobes CD, Hall A. Rho, Rac, and Cdc42 Gtpases Regulate the Assembly of Multimolecular Focal Complexes Associated with Actin Stress Fibers, Lamellipodia, and Filopodia. Cell 1995;81(1):53-62
   PubMed Web of Science ®Google Scholar
• Ridley AJ, Paterson HF, Johnston CL, et al. The small GTP-binding protein rac regulates growth factor-induced membrane ruffling. Cell 1992;70(3):401-10
   PubMed Web of Science ®Google Scholar
• Ridley AJ, Hall A. The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 1992;70(3):389-99
   PubMed Web of Science ®Google Scholar
• Musch A, Cohen D, Kreitzer G, Rodriguez-Boulan E. cdc42 regulates the exit of apical and basolateral proteins from the trans-Golgi network. EMBO J 2001;20(9):2171-9
   PubMed Web of Science ®Google Scholar
• Olson MF, Ashworth A, Hall A. An essential role for Rho, Rac, and Cdc42 GTPases in cell cycle progression through G1. Science 1995;269(5228):1270-2
   PubMed Web of Science ®Google Scholar
• Chu YS, Thomas WA, Eder O, et al. Force measurements in E-cadherin-mediated cell doublets reveal rapid adhesion strengthened by actin cytoskeleton remodeling through Rac and Cdc42. J Cell Biol 2004;167(6):1183-94
   PubMed Web of Science ®Google Scholar
• Raptis L, Arulanandam R, Geletu M, Turkson J. The R(h)oads to Stat3: stat3 activation by the Rho GTPases. Exp Cell Res 2011;317(13):1787-95
   PubMed Web of Science ®Google Scholar
• Fidyk N, Wang JB, Cerione RA. Influencing cellular transformation by modulating the rates of GTP hydrolysis by Cdc42. Biochemistry 2006;45(25):7750-62
   Google Scholar
• Lin R, Bagrodia S, Cerione R, Manor D. A novel Cdc42Hs mutant induces cellular transformation. Curr Biol 1997;7(10):794-7
   Google Scholar
• Kamai T, Yamanishi T, Shirataki H, et al. Overexpression of RhoA, Rac1, and Cdc42 GTPases is associated with progression in testicular cancer. Clin Cancer Res 2004;10(14):4799-805
   PubMed Web of Science ®Google Scholar
• Tucci MG, Lucarini G, Brancorsini D, et al. Involvement of E-cadherin, beta-catenin, Cdc42 and CXCR4 in the progression and prognosis of cutaneous melanoma. Br J Dermatol 2007;157(6):1212-16
   PubMed Web of Science ®Google Scholar
• Reymond N, Im JH, Garg R, et al. Cdc42 promotes transendothelial migration of cancer cells through beta1 integrin. J Cell Biol 2012;199(4):653-68
   PubMed Web of Science ®Google Scholar
• Lash AE, Tolstoshev CM, Wagner L, et al. SAGEmap: a Public Gene Expression Resource. Genome Res 2000;10(7):1051-60
   PubMed Web of Science ®Google Scholar
• Hart MJ, Eva A, Evans T, et al. Catalysis of guanine nucleotide exchange on the CDC42Hs protein by the dbl oncogene product. Nature 1991;354(6351):311-14
   Google Scholar
• Citterio C, Menacho-Marquez M, Garcia-Escudero R, et al. The rho exchange factors vav2 and vav3 control a lung metastasis-specific transcriptional program in breast cancer cells. Sci Signal 2012;5(244):ra71
   PubMed Web of Science ®Google Scholar
• Chang KH, Sanchez-Aguilera A, Shen S, et al. Vav3 collaborates with p190-BCR-ABL in lymphoid progenitor leukemogenesis, proliferation, and survival. Blood 2012;120(4):800-11
   Google Scholar
• Lin KT, Gong J, Li CF, et al. Vav3-rac1 signaling regulates prostate cancer metastasis with elevated Vav3 expression correlating with prostate cancer progression and posttreatment recurrence. Cancer Res 2012;72(12):3000-9
   Google Scholar
• Meller N, Merlot S, Guda C. CZH proteins: a new family of Rho-GEFs. J Cell Sci 2005;118(Pt 21):4937-46
   Google Scholar
• McGhee SA, Chatila TA. DOCK8 immune deficiency as a model for primary cytoskeletal dysfunction. Dis Markers 2010;29(3-4):151-6
   PubMedGoogle Scholar
• Tcherkezian J, Lamarche-Vane N. Current knowledge of the large RhoGAP family of proteins. Biol Cell 2007;99(2):67-86
   PubMed Web of Science ®Google Scholar
• Lahoz A, Hall A. A tumor suppressor role for srGAP3 in mammary epithelial cells. Oncogene 2012
   Google Scholar
• Garcia-Mata R, Boulter E, Burridge K. The 'invisible hand': regulation of RHO GTPases by RHOGDIs. Nat Rev Mol Cell Biol 2011;12(8):493-504
   PubMed Web of Science ®Google Scholar
• Zhao L, Wang H, Li J, et al. Overexpression of Rho GDP-dissociation inhibitor alpha is associated with tumor progression and poor prognosis of colorectal cancer. J Proteome Res 2008;7(9):3994-4003
   PubMed Web of Science ®Google Scholar
• Zhao L, Wang H, Sun X, Ding Y. Comparative proteomic analysis identifies proteins associated with the development and progression of colorectal carcinoma. FEBS J 2010;277(20):4195-204
   PubMed Web of Science ®Google Scholar
• Fritz G, Lang P, Just I. Tissue-specific variations in the expression and regulation of the small GTP-binding protein Rho. Biochim Biophys Acta 1994;1222(3):331-8
   Google Scholar
• Jiang WG, Watkins G, Lane J, et al. Prognostic value of rho GTPases and rho guanine nucleotide dissociation inhibitors in human breast cancers. Clin Cancer Res 2003;9(17):6432-40
   Google Scholar
• Ding J, Huang S, Wu S, et al. Gain of miR-151 on chromosome 8q24.3 facilitates tumour cell migration and spreading through downregulating RhoGDIA. Nat Cell Biol 2010;12(4):390-9
   PubMed Web of Science ®Google Scholar
• Gildea JJ, Seraj MJ, Oxford G, et al. RhoGDI2 is an invasion and metastasis suppressor gene in human cancer. Cancer Res 2002;62(22):6418-23
   PubMed Web of Science ®Google Scholar
• Niu H, Li H, Xu C, He P. Expression profile of RhoGDI2 in lung cancers and role of RhoGDI2 in lung cancer metastasis. Oncol Rep 2010;24(2):465-71
   Google Scholar
• Ma L, Xu G, Sotnikova A, et al. Loss of expression of LyGDI (ARHGDIB), a rho GDP-dissociation inhibitor, in Hodgkin lymphoma. Br J Haematol 2007;139(2):217-23
   Google Scholar
• Stevens EV, Banet N, Onesto C, et al. RhoGDI2 antagonizes ovarian carcinoma growth, invasion and metastasis. Small GTPases 2011;2(4):202-10
   PubMedGoogle Scholar
• Zhang Y, Zhang B. D4-GDI, a Rho GTPase regulator, promotes breast cancer cell invasiveness. Cancer Res 2006;66(11):5592-8
   PubMed Web of Science ®Google Scholar
• Hu LD, Zou HF, Zhan SX, Cao KM. Biphasic expression of RhoGDI2 in the progression of breast cancer and its negative relation with lymph node metastasis. Oncol Rep 2007;17(6):1383-9
   Google Scholar
• Lin Q, Fuji RN, Yang W, Cerione RA. RhoGDI is required for Cdc42-mediated cellular transformation. Curr Biol 2003;13(17):1469-79
   Google Scholar
• Cotteret S, Chernoff J. The evolutionary history of effectors downstream of Cdc42 and Rac. Genome Biol 2002;3(2):REVIEWS0002
   Google Scholar
• Dummler B, Ohshiro K, Kumar R, Field J. Pak protein kinases and their role in cancer. Cancer Metastasis Rev 2009;28(1-2):51-63
   PubMed Web of Science ®Google Scholar
• Chow HY, Jubb AM, Koch JN, et al. p21-Activated kinase 1 is required for efficient tumor formation and progression in a Ras-mediated skin cancer model. Cancer Res 2012;72(22):5966-75
   PubMed Web of Science ®Google Scholar
• Arias-Romero LE, Villamar-Cruz O, Huang M, et al. PAK1 kinase links ErbB2 to beta-catenin in transformation of breast epithelial cells. Cancer Res 2013;73(12):3671-82
   Google Scholar
• Chan PM, Manser E. PAKs in human disease. Prog Mol Biol Transl Sci 2012;106:171-87
   Google Scholar
• Callow MG, Clairvoyant F, Zhu S, et al. Requirement for PAK4 in the anchorage-independent growth of human cancer cell lines. J Biol Chem 2002;277(1):550-8
   PubMed Web of Science ®Google Scholar
• Liu Y, Xiao H, Tian Y, et al. The pak4 protein kinase plays a key role in cell survival and tumorigenesis in athymic mice. Mol Cancer Res 2008;6(7):1215-24
   PubMed Web of Science ®Google Scholar
• Ahn HK, Jang J, Lee J, et al. P21-activated kinase 4 overexpression in metastatic gastric cancer patients. Transl Oncol 2011;4(6):345-9
   PubMed Web of Science ®Google Scholar
• Siu MK, Chan HY, Kong DS, et al. p21-activated kinase 4 regulates ovarian cancer cell proliferation, migration, and invasion and contributes to poor prognosis in patients. Proc Natl Acad Sci 2010;107(43):18622-7
   PubMed Web of Science ®Google Scholar
• Liu Y, Chen N, Cui X, et al. The protein kinase Pak4 disrupts mammary acinar architecture and promotes mammary tumorigenesis. Oncogene 2010;29(44):5883-94
   Google Scholar
• Arias-Romero LE, Chernoff J. A tale of two Paks. Biol Cell 2008;100(2):97-108
   PubMed Web of Science ®Google Scholar
• Mishra R, Barthwal MK, Sondarva G, et al. Glycogen synthase kinase-3beta induces neuronal cell death via direct phosphorylation of mixed lineage kinase 3. J Biol Chem 2007;282(42):30393-405
   Google Scholar
• Rangasamy V, Mishra R, Mehrotra S, et al. Estrogen suppresses MLK3-mediated apoptosis sensitivity in ER+ breast cancer cells. Cancer Res 2010;70(4):1731-40
   Google Scholar
• Mishra P, Senthivinayagam S, Rangasamy V, et al. Mixed lineage kinase-3/JNK1 axis promotes migration of human gastric cancer cells following gastrin stimulation. Mol Endocrinol 2010;24(3):598-607
   Google Scholar
• Zhan Y, Modi N, Stewart AM, et al. Regulation of mixed lineage kinase 3 is required for Neurofibromatosis-2-mediated growth suppression in human cancer. Oncogene 2011;30(7):781-9
   Google Scholar
• Chen Q, Hongu T, Sato T, et al. Key roles for the lipid signaling enzyme phospholipase d1 in the tumor microenvironment during tumor angiogenesis and metastasis. Sci signal 2012;5(249):ra79
   Google Scholar
• Mahajan K, Challa S, Coppola D, et al. Effect of Ack1 tyrosine kinase inhibitor on ligand-independent androgen receptor activity. Prostate 2010;70(12):1274-85
   Google Scholar
• Chua BT, Lim SJ, Tham SC, et al. Somatic mutation in the ACK1 ubiquitin association domain enhances oncogenic signaling through EGFR regulation in renal cancer derived cells. Mol Oncol 2010;4(4):323-34
   PubMed Web of Science ®Google Scholar
• Howlin J, Rosenkvist J, Andersson T. TNK2 preserves epidermal growth factor receptor expression on the cell surface and enhances migration and invasion of human breast cancer cells. Breast Cancer Res 2008;10(2):R36
   Google Scholar
• van der Horst EH, Degenhardt YY, Strelow A, et al. Metastatic properties and genomic amplification of the tyrosine kinase gene ACK1. Proc Natl Acad Sci USA 2005;102(44):15901-6
   Google Scholar
• Jadeski L, Mataraza JM, Jeong HW, et al. IQGAP1 stimulates proliferation and enhances tumorigenesis of human breast epithelial cells. J Biol Chem 2008;283(2):1008-17
   Google Scholar
• Sun W, Zhang K, Zhang X, et al. Identification of differentially expressed genes in human lung squamous cell carcinoma using suppression subtractive hybridization. Cancer Lett 2004;212(1):83-93
   Google Scholar
• Bertucci F, Salas S, Eysteries S, et al. Gene expression profiling of colon cancer by DNA microarrays and correlation with histoclinical parameters. Oncogene 2004;23(7):1377-91
   Google Scholar
• White CD, Brown MD, Sacks DB. IQGAPs in cancer: a family of scaffold proteins underlying tumorigenesis. FEBS Lett 2009;583(12):1817-24
   Google Scholar
• Jin SH, Akiyama Y, Fukamachi H, et al. IQGAP2 inactivation through aberrant promoter methylation and promotion of invasion in gastric cancer cells. Int J Cancer 2008;122(5):1040-6
   PubMed Web of Science ®Google Scholar
• Schmidt VA, Chiariello CS, Capilla E, et al. Development of hepatocellular carcinoma in Iqgap2-deficient mice is IQGAP1 dependent. Mol Cell Biol 2008;28(5):1489-502
   PubMedGoogle Scholar
• Brill L, Eblen TS, Periasamy A, et al. Protein-protein interactions in fixed cells and glial tumors revealed by antibody-based fluorescence resonance energy transfer (FRET). Faseb J 2006;20(5):A1088-A89
   Google Scholar
• Zhou R, Guo Z, Watson C, et al. Polarized distribution of IQGAP proteins in gastric parietal cells and their roles in regulated epithelial cell secretion. Mol Biol Cell 2003;14(3):1097-108
   Google Scholar
• Yamashiro S, Noguchi T, Mabuchi I. Localization of two IQGAPs in cultured cells and early embryos of Xenopus laevis. Cell Motil Cytoskeleton 2003;55(1):36-50
   Google Scholar
• Bryant DM, Datta A, Rodriguez-Fraticelli AE, et al. A molecular network for de novo generation of the apical surface and lumen. Nat Cell Biol 2010;12(11):1035-45
   PubMed Web of Science ®Google Scholar
• Jaffe AB, Kaji N, Durgan J, Hall A. Cdc42 controls spindle orientation to position the apical surface during epithelial morphogenesis. J Cell Biol 2008;183(4):625-33
   PubMed Web of Science ®Google Scholar
• Lu Q, Longo FM, Zhou H, et al. Signaling through Rho GTPase pathway as viable drug target. Curr Med Chem 2009;16(11):1355-65
   PubMed Web of Science ®Google Scholar
• Murray BW, Guo C, Piraino J, et al. Small-molecule p21-activated kinase inhibitor PF-3758309 is a potent inhibitor of oncogenic signaling and tumor growth. Proc Natl Acad Sci 2010;107(20):9446-51
   PubMed Web of Science ®Google Scholar
• Pitts TM, Kulikowski GN, Tan AC, et al. Association of the epithelial-to-mesenchymal transition phenotype with responsiveness to the p21-activated kinase inhibitor, PF-3758309, in colon cancer models. Front Pharmacol 2013;4:35
   PubMed Web of Science ®Google Scholar
• Bradshaw-Pierce EL, Pitts TM, Tan AC, et al. Tumor P-Glycoprotein Correlates with Efficacy of PF-3758309 in in vitro and in vivo Models of Colorectal Cancer. Front Pharmacol 2013;4:22
   PubMed Web of Science ®Google Scholar
• Ong CC, Jubb AM, Jakubiak D, et al. P21-activated kinase 1 (PAK1) as a therapeutic target in BRAF wild-type melanoma. J Natl Cancer Inst 2013;105(9):606-7
   Google Scholar
• Pelish HE, Peterson JR, Salvarezza SB, et al. Secramine inhibits Cdc42-dependent functions in cells and Cdc42 activation in vitro. Nat Chem Biol 2006;2(1):39-46
   Google Scholar
• Friesland A, Zhao Y, Chen YH, et al. Small molecule targeting Cdc42-intersectin interaction disrupts Golgi organization and suppresses cell motility. Proc Natl Acad Sci 2013;110(4):1261-6
   Google Scholar
• Hong L, Kenney SR, Phillips GK, et al. Characterization of a cdc42 protein inhibitor and its use as a molecular probe. J Biol Chem 2013;288(12):8531-43
   Google Scholar