Erratum: Cdc42 is not essential for filopodium formation, directed migration, cell polarization, and mitosis in fibroblastoid cells (Molecular Biology of the Cell (2005) 16 (4473-4484) DOI: 10.1091/mbc.E05-01-0061);Cdc42 is not essential for filopodium formation, directed migration, cell polarization, and mitosis in fibroblastoid cells

Molecular Biology of the Cell

Volumn 16, Issue 10, 2005, Pages 4473-4484

  Czuchra, Aleksandra ^a   Wu, Xunwei ^a   Meyer, Hannelore ^a   Van Hengel, Jolanda ^a,b   Schroeder, Timm ^c   Geffers, Robert ^d   Rottner, Klemens ^d   Brakebusch, Cord ^a  

^a MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

^b GHENT UNIVERSITY   (Belgium)

^c INSTITUTE OF EPIDEMIOLOGY   (Germany)

^d HELMHOLTZ CENTRE FOR INFECTION RESEARCH   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

GUANOSINE TRIPHOSPHATASE; PROTEIN CDC42;

ANIMAL CELL; ARTICLE; CELL MIGRATION; CELL POLARITY; CELL SHAPE; CYTOSKELETON; FIBROBLAST; FILOPODIUM; GENE INACTIVATION; GOLGI COMPLEX; MEMBRANE TRANSPORT; MITOSIS; NONHUMAN; ORIENTATION; POLARIZATION; PRIORITY JOURNAL; PROTEIN FUNCTION;

EID: 26244449496     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E05-01-0061     Document Type: Erratum

References (37)

1. Abe, T., Kato, M., Miki, H., Takenawa, T., and Endo, T. (2003). Small GTPase Tc10 and its homologue RhoT induce N-WASP-mediated long process formation and neurite outgrowth. J. Cell Sci. 116, 155-168.
2. Aspenström, P., Fransson, A., and Saras, J. (2004). Rho GTPases have diverse effects on the organization of the actin filament system. Biochem. J. 377, 327-337.
3. Bishop, A. L., and Hall, A. (2000). Rho GTPases and their effector proteins. Biochem. J. 348, 241-255.
4. Bokoch, G. M. (2003). Biology of the p21-activated kinases. Annu. Rev. Biochem. 72, 743-781.
5. Braga, V. M., Betson, M., Li, X., and Lamarche-Vane, N. (2000). Activation of the small GTPase Rac is sufficient to disrupt cadherin-dependent cell-cell adhesion in normal human keratinocytes. Mol. Biol. Cell. 11, 3703-3721.
6. Carl, U. D., Pollmann, M., Orr, E., Gertler, F. B., Chakraborty, T., and Wehland, J. (1999). Aromatic and basic residues within the EVH1 domain of VASP specify its interaction with proline-rich ligands. Curr. Biol. 9, 715-718.
7. Chen, F. et al. (2000). Cdc42 is required for PIP2 induced actin polymerization and early development but not for cell viability. Curr. Biol. 10, 758-765.
8. Eggert, U. S., Kiger, A. A., Richter, C., Perlman, Z. E., Perrimon, N., Mitchison, T. J., and Field, C. M. (2004). Parallel chemical genetic and genome-wide RNAi screens identify cytokinesis inhibitors and targets. PLoS Biol. 2, e379.
9. Ellis, S., and Mellor, H. (2000). The novel Rho-family GTPase Rif regulates coordinated actin-based membrane rearrangements. Curr. Biol. 10, 1387-1390.
10. Etienne-Manneville, S., and Hall, A. (2001). Integrin-mediated activation of Cdc42 controls cell polarity in migrating astrocytes through protein kinase Cζ. Cell 106, 489-498.
11. Etienne-Manneville, S., and Hall, A. (2003). Cdc42 regulates GSK-3β and adenomatous polyposis coli to control cell polarity. Nature 421, 753-756.
12. Feig, L. A. (1999). Tools of the trade: use of dominant-inhibitory mutants of Ras-family GTPases. Nat. Cell Biol. 1, E25-E27.
13. Frost, J. A., Steen, H., Shapiro, P., Lewis, T., Ahn, N., Shaw, P. E., and Cobb, M. H. (1997). Cross-cascade activation of ERKs and ternary complex factors by Rho family proteins. EMBO J. 16, 6426-6438.
14. Fujikura, J., Yamato, E., Yonemura, S., Hosoda, K., Masui, S., Nakao, K., Miyazaki, J., and Niwa, H. (2002). Differentiation of embryonic stem cells is induced by GATA factors. Genes Dev. 16, 784-789.
15. Fukata, M., Nakagawa, M., and Kaibuchi, K. (2003). Roles of Rho-family GTPases in cell polarisation and directional migration. Curr. Opin. Cell Biol. 15, 590-597.
16. Gauthier-Rouvière, C., Vignal, E., Mériane, M., Roux, P., Montcourier, P., and Fort, P. (1998). RhoG GTPase controls a pathway that independently activates Rac1 and Cdc42Hs. Mol. Biol. Cell 9, 1379-1394.
17. Haraguchi, T., Ding, D-Q., Yamamoto, A., Kaneda, T., Koujin, T., and Hiraoka, Y. (1999). Multiple-color fluorescence imaging of chromosomes and microtubules in living cells. Cell Struct. Funct. 24, 291-298.
18. Kozma, R., Ahmed, S., Best, A., and Lim, L. (1995). The Ras-related protein Cdc42Hs and bradykinin promote formation of peripheral actin microspikes and filopodia in Swiss 3T3 fibroblasts. Mol. Cell. Biol. 15, 1942-1952.
19. Murphy, G. A., Solski, P. A., Jillian, S. A., Pérez de la Ossa, P., D'Eustachio, P., Der, C. J., and Rush, M. G. (1999). Cellular functions of TC10, a Rho family GTPase: regulation of morphology, signal transduction and cell growth. Oncogene 18, 3831-3845.
20. Neudauer, C. L., Joberty, G., Tatsis, N., and Macara, I. G. (1998). Distinct cellular effects and interactions of the Rho-family GTPase TC10. Curr. Biol. 8, 1151-1160.
21. Nobes, C. D., and Hall, A. (1995). Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell 81, 53-62.
22. Nobes, C. D., and Hall, A. (1999). Rho GTPases control polarity, protrusion, and adhesion during cell movement. J. Cell Biol. 144, 1235-1244.
23. Paulsson, M., Aumalley, M., Deutzmann, R., Timpl, R., Beck, K., and Engel, J. (1987). Laminin-nidogen complex. Extraction with chelating agents and structural characterization. Eur. J. Biochem. 166, 11-19.
24. Rios, R. M., and Bornens, M. (2003). The Golgi apparatus at the cell centre. Curr. Opin. Cell Biol. 15, 60-66.
25. Rottner, K., Behrendt, B., Small, J. V., and Wehland, J. (1999). VASP dynamics during lamellipodia protrusion. Nat. Cell Biol. 1, 321-322.
26. Saras, J., Wollberg, P., and Aspenström, P. (2004). Wrch1 is a GTPase-deficient Cdc42-like protein with unusual binding characteristics and cellular effects. Exp. Cell Res. 299, 356-369.
27. Schmidt, A., and Hall, A. (2002). Guanine nucleotide exchange factors for Rho GTPases: turning on the switch. Genes Dev. 16, 1587-1609.
28. Small, J. V., Stradal, T., Vignal, E., and Rottner, K. (2002). The lamellipodium: where motility begins. Trend Cell Biol. 12, 112-120.
29. Stramer, B., Wood, W., Galko, M. J., Redd, M. J., Jacinto, A., Parkhurst, S. M., and Martin, P. (2005). Live imaging of wound inflammation in Drosophila embryos reveals key roles for small GTPases during in vivo cell migration. J. Cell Biol. 168, 567-573.
30. Tao, W., Pennica, D., Xu, L., Kalejta, R.F., and Levine, A. J. (2001). Wrch-1, a novel member of the Rho gene family that is regulated by Wnt-1. Genes Dev. 15, 1796-1807.
31. Vignal, E., De Toledo, M., Comunale, F., Ladopoulou, A., Gauthier-Rouvière, C., Blangy, A., and Fort, P. (2000). Characterization of TCL, a new GTPase of the rho family related to TC10 and Ccdc42. J. Biol. Chem. 275, 36457-36464.
32. Watanabe, T., Wang, S., Noritake, J., Sato, K., Fukata, M., Takefuji, M., Nakagawa, M., Izumi, N., Akiyama, T., and Kaibuchi, K. (2004). Interaction with IQGAP1 links APC to Rac1, Cdc42, and actin filaments during cell polarization and migration Dev. Cell 7, 871-883.
33. Wennerberg, K., and Der, C. J. (2004). Rho-family GTPases: it's not only Rac and Rho (and I like it). J. Cell Sci. 117, 1301-1312.
34. Yasuda, S., Oceguera-Yanez, F., Kato, T., Okamoto, M., Yonemura, S., Terada, Y., Ishizaki, T., and Narumiya, S. (2004). Cdc42 and mDia3 regulate microtubule attachment to kinetochores. Nature 428, 767-771.
35. Yatohgo, T., Izumi, I., Kashiwagi, H., and Hayashi, M. (1988). Novel purification of vitronectin from human plasma by heparin affinity chromatography. Cell Struct. Funct. 13, 281-292.
36. Zondag, G. C., Evers, E. E., ten Klooster, J. P., Janssen, L., van der Kammen, R. A., and Collard, J. G. (2000). Oncogenic Ras downregulates Rac activity, which leads to increased Rho activity and epithelial-mesenchymal transition. J. Cell Biol. 149, 775-778.
37. Zugasti, O., Rul, W., Roux, P., Peyssonnaux, C., Eychene, A., Franke, T. F., Fort, P., and Hibner, U. (2001). Raf-MEK-Erk cascade in anoikis is controlled by Rac1 and Cdc42 via Akt. Mol. Cell Biol. 21, 6706-6717.