82
Views
68
CrossRef citations to date
0
Altmetric
Cell Growth and Development

Intermolecular and Intramolecular Interactions Regulate Catalytic Activity of Myotonic Dystrophy Kinase-Related Cdc42-Binding Kinase α

, , &
Pages 2767-2778 | Received 05 Oct 2000, Accepted 31 Jan 2001, Published online: 28 Mar 2023

REFERENCES

  • Ahmed, S., J. Lee, R. Kozma, A. Best, C. Monfries, and L. Lim. 1993. A novel functional target for tumor-promoting phorbol esters and lysophosphatidic acid. The p21rac-GTPase activating protein n-chimaerin. J. Biol. Chem. 268:10709–10712.
  • Amano, M., K. Chihara, N. Nakamura, Y. Fukata, T. Yano, M. Shibata, M. Ikebe, and K. Kaibuchi. 1998. Myosin II activation promotes neurite retraction during the action of Rho and Rho-kinase. Genes Cells 3:177–188.
  • Amano, M., K. Chihara, N. Nakamura, T. Kaneko, Y. Matsuura, and K. Kaibuchi. 1999. The COOH terminus of Rho-kinase negatively regulates Rho-kinase activity. J. Biol. Chem. 274:32418–32424.
  • Aslanidis, C., G. Jansen, C. Amemiya, G. Shutler, M. Mahadevan, C. Tsilfidis, C. Chen, J. Alleman, N. G. M. Wormskamp, M. Vooijs, B. Jessica, K. Johnson, H. J. M. Smeets, G. G. Lennon, A. V. Carrano, R. G. Korneluk, B. Wieringa, and P. J. de Jong. 1992. Cloning of the essential myotonic dystrophy region and mapping of the putative defect. Nature 355:548–551.
  • Atkinson, S. J., and M. Stewart. 1992. Molecular interactions in myosin assembly. Role of the 28-residue charge repeat in the rod. J. Mol. Biol. 226:7–13.
  • Bi, E., and S. H. Zigmond. 1999. Actin polymerization: where the WASP stings. Curr. Biol. 9:R160–R163.
  • Bishop, A., and A. Hall. 2000. Rho GTPases and their effector proteins. Biochem. J. 348:241–255.
  • Bush, E. W., S. M. Helmke, R. A. Birnbaum, and M. B. Perryman. 2000. Myotonic dystrophy protein kinase domains mediate localization, oligomerization, novel catalytic activity, and autoinhibition. Biochemistry 39:8480–8490.
  • Chan, T. O., S. E. Rittenhouse, and P. N. Tsichlis. 1999. AKT/PKB and other D3 phosphoinositide-regulated kinases: kinase activation by phosphoinositide-dependent phosphorylation. Annu. Rev. Biochem. 68:965–1014.
  • Chen, X.-Q., I. Tan, T. Leung, and L. Lim. 1999. The myotonic dystrophy kinase-related Cdc42-binding kinase is involved in the regulation of neurite outgrowth in PC12 cells. J. Biol. Chem. 274:19901–19905.
  • Chihara, K., M. Amano, N. Nakamura, T. Yano, M. Shibata, T. Tokui, H. Ichikawa, R. Ikebe, M. Ikebe, and K. Kaibuchi. 1997. Cytoskeletal rearrangements and transcriptional activation of c-fos serum response element by Rho-kinase. J. Biol. Chem. 272:25121–25127.
  • Ebinu, J. O., D. A. Bottorff, E. Y. W. Chan, S. L. Stang, R. J. Dunn, and J. C. Stone. 1998. RasGRP, a Ras guanyl nucleotide-releasing protein with calcium- and diacylglycerol-binding motifs. 1998. Science 280:1082–1086.
  • Fu, Y.-H., A. Pizzuti, G. Fenwick Jr., J. King, S. Rajnarayan, P. W. Dunne, J. Dubel, G. A. Nasser, T. Ashizawa, P. J. de Jong, B. Wieringa, R. Korneluk, M. B. Perryman, H. F. Epstein, and C. T. Caskey. 1992. An unstable triplet repeat in a gene related to myotonic muscular dystrophy. Science 255:1256–1258.
  • Gallo, G., and P. C. Letourneau. 1998. Axon guidance: GTPases help axons reach their targets. Curr. Biol. 8:R80–R82.
  • Goto, H., H. Kosako, K. Tanabe, M. Yanagida, M. Sakurai, M. Amano, K. Kaibuchi, and M. Inagaki. 1998. Phosphorylation of vimentin by Rho-associated kinase at a unique amino-terminal site that is specifically phosphorylated during cytokinesis. J. Biol. Chem. 273:11728–11736.
  • Gulbins, E., K. M. Coggeshall, G. Baier, D. Telford, C. Langlet, G. Baier-Bitterlich, N. Bonnefoy-Berard, P. Burn, A. Wittinghofer, and A. Altman. 1994. Direct stimulation of Vav guanine nucleotide exchange activity for Ras by phorbol ester and diglycerides. Mol. Cell. Biol. 14:4749–4758.
  • Hall, A.. 1998. Rho GTPases and the actin cytoskeleton. Science 279:509–514.
  • Hirose, M., T. Ishizaki, N. Watanabe, M. Uehata, O. Kranenburg, W. H. Moolenaar, F. Matsumura, M. Maekawa, H. Bito, and S. Narumiya. 1998. Molecular dissection of the Rho-associated protein kinase (p160ROCK)-regulated neurite remodeling in neuroblastoma N1E-115 cells. J. Cell Biol. 141:1625–1636.
  • Ishizaki, T., M. Maekawa, K. Fujisawa, K. Okawa, A. Iwamatsu, A. Fujita, N. Watanabe, Y. Saito, A. Kakizuka, N. Morii, and S. Narumiya. 1996. The small GTP-binding protein Rho binds to and activates a 160 kDa Ser/Thr protein kinase homologous to myotonic dystrophy kinase. EMBO J. 15:1885–1893.
  • Kemp, B. E., M. W. Parker, S. Hu, T. Tiganis, and C. House. 1994. Substrate and pseudosubstrate interactions with protein kinases: determinants of specificity. Trends Biochem. Sci. 19:440–444.
  • Kosako, H., H. Goto, M. Yanagida, K. Matsuzawa, M. Fujita, Y. Tomono, T. Okigaki, H. Odai, K. Kaibuchi, and M. Inagaki. 1999. Specific accumulation of Rho-associated kinase at the cleavage furrow during cytokinesis: cleavage furrow-specific phosphorylation of intermediate filaments. Oncogene 18:2783–2788.
  • Kozma, R., S. Sarner, S. Ahmed, and L. Lim. 1997. Rho family GTPases and neuronal growth cone remodeling: relationship between increased complexity induced by Cdc42Hs, Rac1, and acetylcholine and collapse induced by RhoA and lysophosphatidic acid. Mol. Cell. Biol. 17:1201–1211.
  • Kuroda, S., M. Fukata, M. Nakagawa, K. Fujii, T. Nakamura, T. Ookubo, I. Izawa, T. Nagase, N. Nomura, H. Tani, I. Shoji, Y. Matsuura, S. Yonehara, and K. Kaibuchi. 1998. Role of IQGAP1, a target of the small GTPases Cdc42 and Rac1, in regulation of E-cadherin-mediated cell-cell adhesion. Science 281:832–835.
  • Lam, E.. 1995. Domain analysis of the plant DNA-binding protein GT1a: requirement of four putative α-helices for DNA binding and identification of a novel oligomerization region. Mol. Cell. Biol. 15:1014–1020.
  • Lei, M., W. Lu, W. Meng, M.-C. Parrini, M. J. Eck, B. J. Mayer, and S. C. Harrison. 2000. Structure of PAK in an autoinhibited conformation reveals a multistage activation switch. Cell 102:387–397.
  • Leung, T., X.-Q. Chen, E. Manser, and L. Lim. 1996. The p160 RhoA-binding kinase ROKα is a member of a kinase family and is involved in the reorganization of the cytoskeleton. Mol. Cell. Biol. 16:5313–5327.
  • Leung, T., X.-Q. Chen, I. Tan, E. Manser, and L. Lim. 1998. Myotonic dystrophy kinase-related Cdc42-binding kinase acts as a Cdc42 effector in promoting cytoskeletal reorganization. Mol. Cell. Biol. 18:130–140.
  • Lim, L., E. Manser, T. Leung, and C. Hall. 1996. Regulation of phosphorylation pathways by p21 GTPases: the p21 Ras-related Rho subfamily and its role in phosphorylation signaling pathways. Eur. J. Biochem. 242:171–185.
  • Luo, L., T. Lee, L. Tsai, G. Tang, L. Y. Jan, and Y.-N. Jan. 1997. Genghis Khan (Gek) as a putative effector for Drosophila Cdc42 and regulator of actin polymerization. Proc. Natl. Acad. Sci. USA 94:12963–12968.
  • Maeda, M., C. S. Taft, E. W. Bush, H. Emma, W. M. Bailey, H. Neville, M. B. Perryman, and R. D. Bies. 1995. Identification, tissue-specific expression, and subcellular localization of the 80- and 71-kDa forms of myotonic dystrophy kinase protein. J. Biol. Chem. 270:20246–20249.
  • 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.
  • Matsui, T., M. Amano, T. Yamamoto, K. Chihara, M. Nakafuku, M. Ito, T. Nakano, K. Okawa, A. Iwamatsu, and K. Kaibuchi. 1996. Rho-associated kinase, a novel serine threonine kinase, as a putative target for the small GTP-binding protein Rho. EMBO J. 15:2208–2216.
  • Miki, H., S. Suetsugu, and T. Takenawa. 1998. WAVE, a novel WASP-family protein involved in actin reorganization induced by Rac. EMBO J. 17:6932–6941.
  • Millward, T., D. Hess, and B. A. Hemmings. 1999. Ndr protein kinase is regulated by phosphorylation on two conserved sequence motifs. J. Biol. Chem. 274:33847–33850.
  • Nakano, K., K. Takaishi, A. Kodama, A. Mammoto, H. Shiozaki, M. Monden, and Y. Takai. 1999. Distinct actions and cooperative roles of ROCK and mDia in Rho small G protein-induced reorganization of the actin cytoskeleton in Madin-Darby canine kidney cells. Mol. Biol. Cell 10:2481–2491.
  • Palaty, C. K., G. Kalmar, G. Tai, S. Oh, L. Amankawa, M. Affolter, R. Aebersold, and S. L. Pelech. 1997. Identification of the autophosphorylation sites of the Xenopus laevis Pim-1 proto-oncogene-encoded protein kinase. J. Biol. Chem. 272:10514–10521.
  • Read, R. D., J. M. Lionberger, and T. E. Smithgall. 1997. Oligomerization of the Fes tyrosine kinase. Evidence for a coiled-coil domain in the unique N-terminal region. J. Biol. Chem. 272:18498–18503.
  • Sahai, E., T. Ishizaki, S. Narumiya, and R. Treisman. 1999. Transformation mediated by RhoA requires activity of ROCK kinases. Curr. Biol. 11:136–145.
  • 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.
  • Sin, W. C., X.-Q. Chen, T. Leung, and L. Lim. 1998. RhoA-binding kinase alpha translocation is facilitated by the collapse of the vimentin intermediate filament network. Mol. Cell. Biol. 18:6325–6339.
  • Tolias, K. F., J. H. Hartwig, H. Ishihara, Y. Shibasaki, L. C. Cantley, and C. L. Carpenter. 2000. Type I alpha-phosphatidylinositol-4-phosphate-5-kinase mediates rac-dependent actin assembly. Curr. Biol. 10:153–156.
  • Topham, M. K., and S. M. Prescott. 1999. Mammalian diacylglycerol kinases, a family of lipid kinases with signaling functions. J. Biol. Chem. 274:11447–11450.
  • Van Aelst, L., T. Joneson, and D. Bar-Sagi. 1996. Identification of a novel Rac1-interacting protein involved in membrane ruffling. EMBO J. 15:3778–3786.
  • Waring, J. D., R. Haq, K. Tamai, L. A. Sabourin, J. E. Ikeda, and R. G. Korneluk. 1996. Investigation of myotonic dystrophy kinase isoform translocation and membrane association. J. Biol. Chem. 271:15187–15193.
  • Watanabe, N., T. Kato, A. Fujita, T. Ishizaki, and S. Narumiya. 1999. Cooperation between mDia1 and ROCK in Rho-induced actin reorganization. Nat. Cell Biol. 1:136–143.
  • Weiss, A., and J. Schlessinger. 1998. Switching signals on or off by receptor dimerization. Cell 94:277–280.
  • Wu, S., and R. J. Kaufman. 1997. A model for the double-stranded RNA (dsRNA)-dependent dimerization and activation of the dsRNA-activated protein kinase PKR. J. Biol. Chem. 272:1291–1296.
  • Zhao, Z.-S., E. Manser, X.-Q. Chen, C. Chong, T. Leung, and L. Lim. 1998. A conserved negative regulatory region in αPAK: inhibition of PAK kinases reveals their morphological roles downstream of Cdc42 and Rac1. Mol. Cell. Biol. 18:2153–2163.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.