Requirement of p21-activated kinase (PAK) for Salmonella typhimurium- induced nuclear responses

Journal of Experimental Medicine

Volumn 189, Issue 9, 1999, Pages 1479-1488

  Chen, Li Mei ^a   Bagrodia, Shubha ^b   Cerione, Richard A ^b   Galán, Jorge E ^a  

^a YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b Department of Obstetrics Gynecology   (United States)

Author keywords

Actin cytoskeleton; Bacterial pathogenesis; Cdc42; Signal transduction

Indexed keywords

ACTIN; GUANOSINE TRIPHOSPHATASE; PROTEIN SERINE THREONINE KINASE;

ANIMAL CELL; ARTICLE; CYTOSKELETON; DIARRHEA; ENZYME ACTIVATION; GENE MUTATION; HOST CELL; INTERNALIZATION; NONHUMAN; PRIORITY JOURNAL; SALMONELLA TYPHIMURIUM; SIGNAL TRANSDUCTION;

ANIMALS; CDC42 GTP-BINDING PROTEIN; CELL CYCLE PROTEINS; CELL NUCLEUS; COS CELLS; CYTOSKELETON; ENZYME ACTIVATION; GTP-BINDING PROTEINS; MUTAGENESIS; PROTEIN-SERINE-THREONINE KINASES; SALMONELLA TYPHIMURIUM; SRC HOMOLOGY DOMAINS;

EID: 0033519243     PISSN: 00221007     EISSN: None     Source Type: Journal    
DOI: 10.1084/jem.189.9.1479     Document Type: Article

References (43)

1. Galán, J.E., and J.B. Bliska. 1996. Cross-talk between bacterial pathogens and their host cells. Annu. Rev. Cell Dev. Biol. 12:219-253.
2. Galán, J.E., and P.J. Sansonetti. 1996. Molecular and cellular bases of Salmonella and Shigella interactions with host cells. In Escherichia coli and Salmonella typhimurium Cellular and Molecular Biology, 2nd ed. F.C. Neidhardt, editor. American Society for Microbiology Press, Washington, DC. 2757-2763.
3. Galán, J.E. 1996. Molecular bases of Salmonella entry into host cells. Mol. Microbiol. 20:263-271.
4. Finlay, B.B., and S. Ruschkowski. 1991. Cytoskeletal rearrangements accompanying Salmonella entry into epithelial cells. J. Cell Sci. 99:283-296.
5. Ginocchio, C., J. Pace, and J.E. Galán. 1992. Identification and molecular characterization of a Salmonella typhimurium gene involved in triggering the internalization of salmonellae into cultured epithelial cells. Proc. Natl. Acad. Sci. USA. 89: 5976-5980.
6. Takeuchi, A. 1967. Electron microscopic studies of experimental Salmonella infection. I. Penetration into the intestinal epithelium by Salmonella typhimurium. Am. J. Pathol. 50:109-136.
7. Hobbie, S., L.M. Chen, R. Davis, and J.E. Galán. 1997. Involvement of the mitogen-activated protein kinase pathways in the nuclear responses and cytokine production induced by Salmonella typhimurium in cultured intestinal cells. J. Immunol. 159:5550-5559.
8. Chen, L.M., S. Hobbie, and J.E. Galán. 1996. Requirement of Cdc42 for Salmonella typhimurium-induced cytoskeletal reorganization and nuclear responses in cultured cell. Science. 274:2115-2118.
9. Hardt, W.-D., L.-M. Chen, K.E. Schuebel, X.R. Bustelo, and J.E. Galán. 1998. Salmonella typhimurium encodes an activator of Rho GTPases that induces membrane ruffling and nuclear responses in host cells. Cell. 93:815-826.
10. Minden, A., A. Lin, F.X. Claret, A. Abo, and M. Karin. 1995. Selective activation of the JNK signaling cascade and cJun transcriptional activity by the small GTPases Rac and Cdc42Hs. Cell. 81:1147-1157.
11. Coso, O.A., M. Chiarello, J.-C. Yu, H. Teramoto, P. Crespo, N. Xu, T. Miki, and J.S. Gutkind. 1995. The small GTP-binding proteins Rac1 and Cdc42 regulate the activity of JNK/SAPK signaling pathways. Cell. 81:1137-1146.
12. Dutartre, H., J. Davoust, J.-P. Gorvel, and P. Chavrier. 1996. Cytokinesis and redistribution of actin-cytoskeleton regulatory components in cells expressing the Rho GTPase Cdc42Hs. J. Cell Sci. 109:367-377.
13. Nobes, C.D., and A. Hall. 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.
14. Hall, A. 1998. Rho GTPases and the actin cytoskeleton. Science. 279:509-514.
15. Van Aelst, L., and C. D'Souza-Schorey. 1997. Rho GTPases and signaling networks. Genes Dev. 11:2295-2322.
16. Tapon, N., and A. Hall. 1997. Rho, Rac and Cdc42 GTPases regulate the organization of the actin cytoskeleton. Curr. Opin. Cell Biol. 9:86-92.
17. Hart, M.J., M.G. Callow, B. Souza, and P. Polakis. 1996. IQGAP1, a calmodulin-binding protein with a rasGAP-related domain, is a potential effector for Cdc42Hs. EMBO (Eur. Mol. Biol. Organ.) J. 15:2997-3005.
18. Aspenstrom, P. 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. 7:479-487.
19. Manser, E., T. Leung, H. Salihuddin, Z.-S. Zhao, and L. Lim. 1994. A brain serine/threonine kinase activated by Cdc42 and Rac1. Nature. 367:40-46.
20. Nagata, K.-I., A. Puls, C. Futter, P. Aspenstrom, E. Schaefer, T. Nakata, N. Hirokawa, and A. Hall. 1998. The MAP kinase kinase kinase MLK2 co-localizes with activated JNK along microtubules and associates with kinesin superfamily motor KIF3. EMBO (Eur. Mol. Biol. Organ.) J. 17:149-158.
21. Symons, M., J.M.J. Derry, B. Karlak, S. Jiang, V. Lemahieu, F. McCormick, U. Francke, and A. Abo. 1996. Wiskott-Aldrich syndrome protein, a novel effector for the GTPase Cdc42Hs, is implicated in actin polymerization. Cell. 84: 723-734.
22. Yang, W., and R.A. Cerione. 1997. Cloning and characterization of a novel Cdc42-associated tyrosine kinase, ACK-2, from bovine brain. J. Biol. Chem. 272:24819-24824.
23. Teramoto, H., O.A. Coso, H. Miyata, T. Igishi, T. Miki, and J.S. Gutkind. 1996. Signaling from the small GTP-binding protein Rac-1 and Cdc42 to the cJun N-terminal kinase/ stress-activated protein kinase pathway. J. Biol. Chem. 271: 27225-27228.
24. Burbelo, P.D., D. Drechsel, and A. Hall. 1995. A conserved binding motif defines numerous candidate target proteins for both Cdc42 and Rac GTPases. J. Biol. Chem. 270:29071-29074.
25. Sells, M.A., and J. Chernoff. 1997. Emerging from the Pak: the p21-activated protein kinase family. Trends Cell Biol. 7:162-167.
26. Manser, E., H.-Y. Huang, T.-H. Loo, X.-Q. Chen, J.-M. Dong, T. Leung, and L. Lim. 1997. Expression of constitutively active α-PAK reveals effects of the kinase on actin and focal complexes. Mol. Cell. Biol. 17:1129-1143.
27. Bagrodia, S., S.J. Taylor, C.L. Creasy, J. Chernoff, and R.A. Cerione. 1995. Identification of a mouse p21Cdc42/Rac activated kinase. J. Biol. Chem. 270:22731-22737.
28. Sells, M.A., U.G. Knaus, S. Bagrodia, D.M. Ambrose, G.M. Bokoch, and J. Chernoff. 1997. Human p21-activated kinase (Pak1) regulates actin organization in mammalian cells. Curr. Biol. 7:202-210.
29. Sawai, E.T., I.H. Khan, P.M. Montbriand, B.M. Peterlin, C. Cheng-Mayer, and P.A. Luciw. 1996. Activation of PAK by HIV and SIV Nef: importance for AIDS in rhesus macaques. Curr. Biol. 6:1519-1527.
30. Lu, X., X. Wu, A. Plemenitas, H. Yu, E.T. Sawai, and A. Abo. 1996. Cdc42 and Rac1 are implicated in the activation of the Nef-associated kinase and replication of HIV-1. Curr. Biol. 6:1677-1684.
31. Westwick, J.K., Q.T. Lambert, G.J. Clark, M. Symons, L. Van Aelst, R.G. Pestell, and C.J. Der. 1997. Rac regulation of transformation, gene expression, and actin organization by multiple, PAK-independent pathways. Mol. Cell. Biol. 17: 1324-1335.
32. Lamarche, N., N. Tapon, L. Stowers, P.D. Burbelo, P. Aspenstrom, T. Bridges, J. Chant, and A. Hall. 1996. Rac and Cdc42 induce actin polymerization and G1 cell cycle progression independently of p65PAK and the JNK/SAPK MAP kinase cascade. Cell. 87:519-529.
33. Diekmann, D., C.D. Nobes, P.D. Burbelo, A. Abo, and A. Hall. 1995. Rac GTPase interacts with GAPs and target proteins through multiple effector sites. EMBO (Eur. Mol. Biol. Organ.) J. 14:5297-5305.
34. Joneson, T., M. McDonough, D. Bar-Sagi, and A.L. Van. 1996. RAC regulation of actin polymerization and proliferation by a pathway distinct from Jun kinase. Science. 274:1374-1376.
35. Kaniga, K., J.C. Bossio, and J.E. Galán. 1994. The Salmonella typhimurium invasion genes invF and invG encode homologues to the PuID and AraC family of proteins. Mol. Microbiol. 13:555-568.
36. Chen, C., and H. Okayama. 1987. High-efficiency transformation of mammalian cells by plasmid DNA. Mol. Cell. Biol. 7:2745-2752.
37. Bagrodia, S., B. Dérijard, R.J. Davis, and R.A. Cerione. 1995. Cdc42 and PAK-mediated signaling leads to Jun kinase and p38 mitogen-activated protein kinase activation. J. Biol. Chem. 270:27995-27998.
38. Bokoch, G.M., A.M. Reilly, R.H. Daniels, C.C. King, A. Olivera, S. Spiegel, and U.G. Knaus. 1998. A GTPase-independent mechanism of p21-activated kinase activation. Regulation by sphingosine and other biologically active lipids. J. Biol. Chem. 273:8137-8144.
39. Dharmawardhane, S., L.C. Sanders, S.S. Martin, R.H. Daniels, and G.M. Bokoch. 1997. Localization of p21-activated kinase 1 (PAK1) to pinocytic vesicles and cortical actin structures in stimulated cells. J. Cell Biol. 138:1265-1278.
40. Hardt, W.-D., H. Urlaub, and J.E. Galán. 1998. A target of the centisome 63 type III protein secretion system of Salmonella typhimurium is encoded by a cryptic bacteriophage. Proc. Null. Acad. Sci. USA. 95:2574-2579.
41. Bokoch, G.M., Y. Wang, B.P. Bohl, M.A. Sells, L.A. Quilliam, and U.G. Knaus. 1996. Interaction of the Nck adapter protein with p21-activated kinase (PAK1). J. Biol. Chem. 271:25746-25749.
42. Hotchin, N.A., and A. Hall. 1996. Regulation of the actin cytoskeleton, integrins and cell growth by the Rho family of small GTPases. Cancer Surv. 27:311-322.
43. Brown, J.L., L. Stowers, M. Baer, J. Trejo, S. Coughlin, and J. Chant. 1996. Human Ste20 homologue hPAK1 links GTPase to the JNK MAP kinase pathway. Curr. Biol. 6:598-605.