Cdc42: New roads to travel

Trends in Cell Biology

Volumn 14, Issue 3, 2004, Pages 127-132

  Cerione, Richard A ^a  

^a Department of Obstetrics Gynecology   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EPIDERMAL GROWTH FACTOR RECEPTOR; GROWTH FACTOR RECEPTOR; GUANOSINE TRIPHOSPHATASE; PROTEIN CDC42;

CELL FUNCTION; CELL GROWTH; CELL POLARITY; CYTOSKELETON; HUMAN; NONHUMAN; PRIORITY JOURNAL; REGULATORY MECHANISM; REVIEW; SIGNAL TRANSDUCTION; SURFACE PROPERTY; UBIQUITINATION;

ANIMALS; BIOLOGICAL TRANSPORT; CDC42 GTP-BINDING PROTEIN; CELL DIVISION; HUMANS; RECEPTORS, GROWTH FACTOR; SIGNAL TRANSDUCTION;

EID: 1442274703     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tcb.2004.01.008     Document Type: Review

References (63)

1. Johnson D.I., Pringle J.R. Molecular characterization of CDC42, a Saccharomyces cerevisiae gene involved in the development of cell polarity. J. Cell Biol. 111:1990;143-152.
2. Shinjo K., et al. 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. 87:1990;9853-9857.
3. Drubin D.G. Development of cell polarity in budding yeast. Cell. 65:1991;1093-1096.
4. Johnson D.I. Cdc42: an essential Rho-type GTPase controlling eukaryotic cell polarity. Microbiol. Mol. Biol. Rev. 63:1999;54-105.
5. Nobes C.D., Hall A. Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell. 81:1995;53-62.
6. Kozma R., et al. The Ras-related protein Cdc42Hs and bradykinin promote formation of peripheral actin microspikes and filopodia in Swiss 3T3 fibroblasts. Mol. Cell. Biol. 15:1995;1942-1952.
7. Ridley A.J., et al. The small GTP-binding protein rac regulates growth factor-induced membrane ruffling. Cell. 70:1992;401-410.
8. Ridley A.J., Hall A. The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell. 70:1992;389-399.
9. Zerial M., McBride H. Rab proteins as membrane organizers. Nat. Rev. Mol. Cell Biol. 2:2001;107-117.
10. Pfeffer S.R. Rab GTPases: specifying and deciphering organelle identity and function. Trends Cell Biol. 11:2001;487-491.
11. Serafini T., et al. ADP-ribosylation factor is a subunit of the coat of Golgi-derived COP-coated vesicles: a novel role for a GTP-binding protein. Cell. 67:1991;239-253.
12. Nakano A., Muramatsu M. A novel GTP-binding protein, Sar1p, is involved in transport from the endoplasmic reticulum to the Golgi apparatus. J. Cell Biol. 109:1989;2677-2691.
13. Erickson J.W., et al. Mammalian Cdc42 is a brefeldin A-sensitive component of the Golgi apparatus. J. Biol. Chem. 271:1996;26850-26854.
14. Ziman M., et al. Subcellular localization of Cdc42p, a Saccharomyces cerevisiae GTP-binding protein involved in the control of cell polarity. Mol. Biol. Cell. 4:1993;1307-1316.
15. Richman T.J., et al. Saccharomyces cerevisiae Cdc42p localizes to cellular membranes and clusters at sites of polarized growth. Eukaryot. Cell. 1:2002;458-468.
16. Lowe M., Kreis T. Regulation of membrane traffic in animal cells by COPI. Biochim. Biophys. Acta. 1404:1998;53-66.
17. Nickel W., et al. Vesicular transport: the core machinery of COPI recruitment and budding. J. Cell Sci. 115:2002;3235-3240.
18. Waters M.G., et al. 'Coatomer': a cytosolic protein complex containing subunits of non-clathrin-coated Golgi transport vesicles. Nature. 349:1991;248-251.
19. Bonifacino J.S., Lippincott-Schwartz J. Coat proteins: shaping membrane transport. Nat. Rev. Mol. Cell Biol. 4:2003;409-411.
20. Orci L., et al. Brefeldin A, a drug that blocks secretion, prevents the assembly of non-clathrin-coated buds on Golgi cisternae. Cell. 64:1991;1183-1195.
21. Zhang C., et al. Expression of a dominant allele of human ARF1 inhibits membrane traffic in vivo. J. Cell Biol. 124:1994;289-300.
22. Wu W.J., et al. The γ-subunit of the coatomer complex binds Cdc42 to mediate transformation. Nature. 405:2000;800-804.
23. Fucini R.V., et al. Golgi vesicle proteins are linked to the assembly of an actin complex defined by mAbp1. Mol. Biol. Cell. 13:2002;621-631.
24. Kroschewski R., et al. Cdc42 controls secretory and endocytic transport to the basolateral plasma membrane of MDCK cells. Nat. Cell Biol. 1:1999;8-13.
25. Müsch A., et al. Cdc42 regulates the exit of apical and basolateral proteins from the trans-Golgi network. EMBO J. 20:2001;2171-2179.
26. Luna A., et al. Regulation of protein transport from the Golgi complex to the endoplasmic reticulum by CDC42 and N-WASP. Mol. Biol. Cell. 13:2002;866-879.
27. Eitzen G., et al. Rho1p and Cdc42p act after Ypt7p to regulate vacuole docking. EMBO J. 20:2001;5650-5656.
28. Müller O., et al. Cdc42p functions at the docking stage of yeast vacuole membrane fusion. EMBO J. 20:2001;5657-5665.
29. Lippincott J., Li R. Sequential assembly of myosin II, an IQGAP-like protein, and filamentous actin to a ring structure involved in budding yeast cytokinesis. J. Cell Biol. 140:1998;355-366.
30. Osman M.A., Cerione R.A. Iqg1p, a yeast homolog of the mammalian IQGAPs, mediates Cdc42p effects on the actin cytoskeleton. J. Cell Biol. 142:1998;443-455.
31. Osman M.A., et al. Iqg1p links spatial and secretion landmarks to polarity and cytokinesis. J. Cell Biol. 159:2002;601-611.
32. Zhang X., et al. Cdc42 interacts with the exocyst and regulates polarized secretion. J. Biol. Chem. 276:2001;46745-46750.
33. Hart M.J., et al. Catalysis of guanine nucleotide exchange on the CDC42Hs protein by the dbl oncogene product. Nature. 354:1991;311-314.
34. Whitehead I.P., et al. Dbl family proteins. Biochim. Biophys. Acta. 1332:1997;F1-F23.
35. Hoffman G.R., Cerione R.A. Signaling to the Rho GTPases: networking with the DH domain. FEBS Lett. 513:2002;85-91.
36. Olson M.F., et al. An essential role for Rho, Rac, and Cdc42 GTPases in cell cycle progression through G1. Science. 269:1995;1270-1272.
37. Qiu R.G., et al. Cdc42 regulates anchorage-independent growth and is necessary for Ras transformation. Mol. Cell. Biol. 17:1997;3449-3458.
38. King A.J., et al. The protein kinase Pak3 positively regulates Raf-1 activity through phosphorylation of serine 338. Nature. 396:1998;180-183.
39. Jelinek T., et al. RAS and RAF-1 form a signalling complex with MEK-1 but not MEK-2. Mol. Cell. Biol. 14:1994;8212-8218.
40. Reinstein J., et al. p21 with a phenylalanine 28 - leucine mutation reacts normally with the GTPase activating protein GAP but nevertheless has transforming properties. J. Biol. Chem. 266:1991;17700-17706.
41. Lin R., et al. A novel Cdc42Hs mutant induces cellular transformation. Curr. Biol. 7:1997;794-797.
42. Lin R., et al. Specific contributions of the small GTPases Rho, Rac and Cdc42 to Dbl transformation. J. Biol. Chem. 274:1999;23633-23641.
43. Tu S., et al. Antiapoptotic Cdc42 mutants are potent activators of cellular transformation. Biochemistry. 41:2002;12350-12358.
44. Wu W.J., et al. Activated Cdc42 sequesters c-Cbl and prevents EGF receptor degradation. Cell. 114:2003;715-725.
45. Levkowitz G., et al. c-Cbl/Sli-1 regulates endocytic sorting and ubiquitination of the epidermal growth factor receptor. Genes Dev. 12:1998;3663-3674.
46. Levkowitz G., et al. Ubiquitin ligase activity and tyrosine phosphorylation underlie suppression of growth factor signaling by c-Cbl/Sli-1. Mol. Cell. 4:1999;1029-1040.
47. Bagrodia S., et al. A novel regulator of p21-activated kinases. J. Biol. Chem. 273:1998;23633-23636.
48. Manser E., et al. PAK kinases are directly coupled to the PIX family of nucleotide exchange factors. Mol. Cell. 1:1998;183-192.
49. Flanders J.A., et al. The Cbl proteins are binding partners for the Cool/Pix family of p21-activated kinase-binding proteins. FEBS Lett. 550:2003;119-123.
50. Feng Q., et al. Regulation of the Cool/Pix proteins: key binding partners of the Cdc42/Rac targets, the p21-activated kinases. J. Biol. Chem. 277:2002;5644-5650.
51. Li Z., et al. Directional sensing requires Gβγ-mediated PAK1 and PIXα-dependent activation of Cdc42. Cell. 114:2003;215-227.
52. Yang W., et al. The Cdc42 target ACK2 directly interacts with clathrin and influences clathrin assembly. J. Biol. Chem. 276:2001;17468-17473.
53. Lin Q., et al. The Cdc42 target ACK2 interacts with sorting nexin 9 (SH3PX1) to regulate epidermal growth factor receptor degradation. J. Biol. Chem. 277:2002;10134-10138.
54. Tu S., et al. Epidermal growth factor-dependent regulation of Cdc42 is mediated by the Src tyrosine kinase. J. Biol. Chem. 278:2003;49293-49300.
55. Pucharcos C., et al. The human intersectin genes and their spliced variants are differentially expressed. Biochim. Biophys. Acta. 1521:2001;1-11.
56. Hussain N.K., et al. Splice variants of intersectin are components of the endocytic machinery in neurons and nonneuronal cells. J. Biol. Chem. 274:1999;15671-15677.
57. Hussain N.K., et al. Endocytic protein intersectin-1 regulates actin assembly via Cdc42 and N-WASP. Nat. Cell Biol. 3:2001;927-932.
58. Lin Q., et al. RhoGDI is required for Cdc42-mediated cellular transformation. Curr. Biol. 13:2003;1469-1479.
59. Hart M.J., et al. A GDP dissociation inhibitor that serves as a GTPase inhibitor for the Ras-like protein CDC42Hs. Science. 258:1992;812-815.
60. Collins, R.N. and Brennwald, P. (2000) Rabs. Front. Mol. Biol. 24, 137-175.
61. Joberty G., et al. The cell-polarity protein Par6 links Par3 and the atypical protein kinase C to Cdc42. Nat. Cell Biol. 2:2000;531-539.
62. Qiu R., et al. A human homolog of the C. elegans polarity determinant Par-6 links Rac and Cdc42 to PCKζ signaling and cell transformation. Curr. Biol. 10:2000;697-707.
63. Etienne-Manneville S., Hall A. Cdc42 regulates GSK-3beta and adenomatous polyposis coli to control cell polarity. Nature. 421:2003;753-756.