Identification of a novel, putative Rho-specific GDP/GTP exchange factor and a RhoA-binding protein: Control of neuronal morphology

Journal of Cell Biology

Volumn 137, Issue 7, 1997, Pages 1603-1613

  Gebbink, Martijn F B G ^a,b   Kranenburg, Onno ^a   Poland, Mieke ^a   Van Horck, Francis P G ^a   Houssa, Brahim ^a   Moolenaar, Wouter H ^a  

^a NETHERLANDS CANCER INSTITUTE   (Netherlands)

^b BOSTON CHILDREN S HOSPITAL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE;

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; CELL STRUCTURE; CYTOSKELETON; GENE OVEREXPRESSION; NERVE CELL; NERVE FIBER GROWTH; NONHUMAN; NORTHERN BLOTTING; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN INTERACTION;

AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; CLONING, MOLECULAR; COS CELLS; GTP-BINDING PROTEINS; GUANINE NUCLEOTIDE EXCHANGE FACTORS; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; MOLECULAR SEQUENCE DATA; NERVE TISSUE PROTEINS; NEURONS; PROTEIN BINDING; PROTEINS; RHO GTP-BINDING PROTEINS; SEQUENCE ANALYSIS;

ANIMALIA;

EID: 0030929149     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.137.7.1603     Document Type: Article

References (44)

1. Adamson, P., C.J. Marshall, A. Hall, and P.A. Tilbrook. 1992a. Post-translational modifications of p21rho proteins. J. Biol. Chem. 267:20033-20038.
2. rho proteins. J. Cell Biol. 119:617-627.
3. Ahmed, S., R. Kozma, J. Lee, C. Monfries, N. Harden, and L. Lim. 1991. The cysteine-rich domain of human proteins, neuronal chimaerin, protein kinase C and diacylglycerol kinase binds zinc. Biochem. J. 280:233-241.
4. Chevray, P.M., and D. Natans. 1992. Protein interaction cloning in yeast: identification of mammalian proteins that react with the leucine zipper of jun, Proc. Natl. Acad Sci. USA. 89:5789-5793.
5. Chrzanowska-Wodnicka, M., and K. Burridge. 1996. Rho-stimulated contractility drives the formation of stress fibers and focal adhesions. J. Cell Biol. 133: 1403-1415.
6. Devereux, J., P. Haeberli, and O. Smithies. 1984. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 12:387-395.
7. Durphee, T., K. Becherer, P.-L. Chen, S.-H. Yeh, Y. Yang, and A.E. Kilburn, 1993. The retinoblastoma protein associates with the protein phosphatase type 1 catalytic subunit. Genes & Dev. 7:555-569.
8. Feig, L.A. 1994. Guanine-nucleotide exchange factors: a family of positive regulators of Ras and related GTPases. Curr. Opin. Cell Biol. 6:204-211.
9. Glaven, J.A., I.P. Whitehead, T. Nomanbhoy, R. Kay, and R.A. Cerione. 1996. Lfc and Lsc oncoproteins represent two new guanine nucleotide exchange factors for the Rho GTP-binding protein. J. Biol. Chem. 272:27374-27381.
10. Gurwitz, D., and D.D. Cunningham. 1988. Thrombin modulates and reverses neuroblastoma neurite outgrowth. Proc. Natl. Acad. Sci. USA. 85:3440-3444.
11. Habets, G., E. Scholtes, D. Zuydgeest, R.A. van der Kammen, J. Stam, A. Berns, and J.G. Collard. 1994. Identification of an invasion-inducing gene, Tiam-1, that encodes a protein with homology to GDP-GTP exchangers for Rho-like proteins. Cell. 77:537-549.
12. Hancock, J.F., and A. Hall. 1993. A novel role for RhoGDI as an inhibitor of GAP proteins. EMBO (Eur. Mol. Biol. Organ.) J. 12:1915-1921.
13. Harper, J.W., G.R. Adami, N. Wei, K. Keyomarsi, and S.J. Elledge. 1993. The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases. Cell. 75:805-816.
14. Jalink, K., and W.H. Moolenaar. 1992. Thrombin receptor activation causes rapid neural cell rounding and neurite retraction independent of classic second messengers. J. Cell Biol. 118:411-119.
15. Jalink, K., T. Eichholtz, F.R. Postma, E.J. van Corven, and W.U. Moolenaar. 1993. Lysophosphatidic acid triggers neuronal shape changes via a novel, receptor-mediated signaling pathway: similarity to thrombin action. Cell Growth Differ. 4:247-255.
16. Jalink, K., E.J. van Corven, T. Hengeveld, N. Morii, S. Narumiya, and W.H. Moolenaar. 1994. Inhibition of lysophosphatidate- and thrombin-induced neurite retraction and neuronal cell rounding by ADP ribosylation of the small GTP-binding protein Rho. J. Cell Biol. 126:801-810.
17. Kamata, Y., T. Nishiki, K. Matsumura, T. Hiroi, and S. Kozaki. 1994. Morphological effects, rate of incorporation, and the enzymatic action of Botulinum ADP-ribosyltransferase, known as C3 exoenzyme, on human neuroblastoma GOTO cells. Microbiol. Immunol. 38:421-428.
18. Katayama, M., M. Kawata, Y. Yoshida, T. Horichi, T. Yamamoto, Y. Matsura, and Y. Takai. 1991. The posttranslationally modified C-terminal structure of rhoAp21. J. Biol. Chem. 266:12639-12645.
19. Kimura, K., M. Ito, M. Amano, K. Chihara, Y. Fukata, M. Nakafuku, B. Yamamori, J. Feng, T. Nakano, K. Okawa, A. Iwamatsu, and K. Kaibuchi. 1996. Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rho-kinase). Science (Wash. DC). 273:245-248.
20. Kranenburg, O., V. Scharnhorst, A.J. Van der Eb, and A. Zantema. 1995. Inhibition of cyclin-dependent kinase activity triggers neuronal differentiation of mouse neuroblastoma cells. J. Cell Biol. 131:227-234.
21. Lupas, A., M. Van Dyke, and J. Stock. 1991. Predicting coiled coils from protein sequences. Science (Wash. DC). 252:1162-1164.
22. Machesky, L.M., and A. Hall. 1996. Rho: a connection between membrane signalling and the cytoskeleton. Trends Cell Biol. 6:304-310.
23. Mackay, D.J.G., C.D. Nobes, and A. Hall. 1995. The Rho's progress: a potential role during neuritogenesis for the Rho family of GTPases. Trends Neurosci. 18:496-501.
24. Madaule, P., T. Furuyashiki, T. Reid, T. Ishizaki, G. Watanabe, N. Morii, and S., Narumiya. 1995. A novel partner for the GTP-bound forms of rho and rac. FEBS Lett. 377:243-248.
25. Moolenaar, W.H. 1995. Lysophosphatidic acid, a multifunctional phospholipid messenger. J. Biol. Chem. 270:8944-8951.
26. Munder, T., and P. Fuerst. 1992. The S. cerevisiae CDC25 gene product binds specifically to catalytically inactive Ras proteins in vivo. Mol. Cell. Biol. 12: 2091-2099.
27. Nishiki, T., S. Narumiya, N. Morii, M. Yamamoto, M. Fujiwara, Y. Kamata, G. Sakaguchi, and S. Kozaki. 1990. ADP-ribosylation of the rho/rac proteins induces growth inhibition, neurite outgrowth and acetylcholine esterase in cultured PC12 cells. Biochem. Biophys. Res. Commun. 167:265-272.
28. Paterson, H.F., A. Self, M.D. Garrett, I. Just, K. Aktories, and A. Hall. 1990. Microinjection of recombinant p21 rho induces rapid changes in cell morphology. J. Cell Biol. 111:1001-1007.
29. Posnett, D.N., H. McGrath, and J.P. Tam. 1988. A novel method of producing anti-peptide antibodies. J. Biol. Chem. 263:1719-1725.
30. Postma, F.R., K. Jalink, T. Hengeveld, and W.H. Moolenaar. 1996. Sphingosine-1-phosphate rapidly induces Rho-dependent neurite retraction: action through a specific cell surface receptor. EMBO (Eur. Mol. Biol. Organ.) J. 15:2388-2395.
31. Quilliam, L.A., R. Khosravi-Far, S.Y. Huff, and C.J. Der. 1995. Guanine nucleotide exchange factors: activators of the Ras superfamily of proteins. Bioessays 17:395104.
32. Ren, X.-D., G.M. Bokoch, A. Traynor-Kapln, G.H. Jenkins, R.A. Anderson, and M.A. Schwartz. 1996. Physical association of the small GTPase Rho with a 68-kda phoshatidylinositol-5 kinase in Swiss 3T3 cells. Mol. Biol. Cell. 7: 435-442.
33. Ridley, A.J., 1996. Rho: themes and variations. Curr. Biol. 6:1256-1264.
34. Ridley, A.J., and A. Hall. 1992. The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell. 70:389-399.
35. Schiestl, R.H., and R.D. Gietz. 1989. High efficiency transformation of intact yeast cells using single stranded nucleic acid as a carrier. Nucleic Acids Res. 18:1068.
36. Suidan, H.S., S.R. Stone, B.A. Hemmings, and D. Monard. 1992. Thrombin causes neunte retraction in neuronal cells through activation of cell surface receptors. Neuron. 8:363-375.
37. Symons, M. 1996. Rho family GTPases: the cytoskeleton and beyond. Trends Biochem. Sci. 21:178-181.
38. Tigyi, G., and R. Miledi. 1992. Lysophosphatidates bound to serum albumin activate membrane currents in Xenopus oocytes and neurite retraction in PC12 pheochromocytoma cells. J. Biol. Chem. 267:21360-21367.
39. 2+ signaling and Rho. J. Neurochem. 66:537-548.
40. Toksoz, D., and D.A. Williams. 1995. Novel oncogene lbc detected by transfection with distinct homology regions to signal transduction products. Oncogene. 9:621-628.
41. Vincent, S., and J. Settleman. 1997. The PRK2 kinase is a potential effector target of both Rho and Rac GTPases and regulates actin cytoskeletal organization. Mol. Cell. Biol. 17:2247-2256.
42. Whitehead, I., H. Kirk, C. Tognom, G. Trigo-Gonzalez, and R. Kay. 1995. Expression cloning of lfc, a novel oncogene with structural similarities to guanine nucleotide exchange factors and to the regulatory region of protein kinase C. J. Biol. Chem. 270:18388-18395.
43. Zheng, Y., M.F. Olson, A. Hall, R.A. Cerione, and D. Toksoz. 1995. Direct involvement of the small GTP-binding protein Rho in lbc oncogene function. J. Biol. Chem. 270:9031-9034.
44. Zondag, G.C.M., W.H. Moolenaar, and M.F.B.G. Gebbink. 1996. Lack of association between receptor tyrosine phosphatase RPTPμ and cadherins. J. Cell Biol. 134:1513-1517.