Caspase-3-mediated cleavage of ROCK I induces MLC phosphorylation and apoptotic membrane blebbing (original) (raw)

• Rao, L., Perez, D. & White, E. Lamin proteolysis facilitates nuclear events during apoptosis. J. Cell. Biol. 135, 1441–1455 (1996).
  Article CAS Google Scholar
• Enari, M. et al. A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD. Nature 391, 43–50 (1998) (published erratum Nature 393, 396).
  Article CAS Google Scholar
• Liu, X., Zou, H., Slaughter, C. & Wang, X. DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis. Cell 89, 175–184 (1997).
  Article CAS Google Scholar
• Rudel, T. & Bokoch, G. M. Membrane and morphological changes in apoptotic cells regulated by caspase-mediated activation of PAK2. Science 276, 1571–1574 (1997).
  Article CAS Google Scholar
• Lee, N. et al. Activation of hPAK65 by caspase cleavage induces some of the morphological and biochemical changes of apoptosis. Proc. Natl Acad. Sci. USA 94, 13642–13647 (1997).
  Article CAS Google Scholar
• Rudolf, E., Peychl, J., Novak, J. & Cervinka, M. Apoptosis — when the cells begin to dance. Front. Biosci. 5, F1–F2 (2000).
  Article CAS Google Scholar
• Kerr, J. F., Winterford, C. M. & Harmon, B. V. Apoptosis. Its significance in cancer and cancer therapy. Cancer 73, 2013–2026 (1994) (published erratum Cancer 73, 3108).
  Article CAS Google Scholar
• Majno, G. & Joris, I. Apoptosis, oncosis, and necrosis. An overview of cell death. Am. J. Pathol. 146, 3–15 (1995).
  CAS Google Scholar
• Zheng, T. S. et al. Caspase-3 controls both cytoplasmic and nuclear events associated with Fas-mediated apoptosis in vivo. Proc. Natl Acad. Sci. USA 95, 13618–13623 (1998).
  Article CAS Google Scholar
• Janicke, R. U., Ng, P., Sprengart, M. L. & Porter, A. G. Caspase-3 is required for alpha-fodrin cleavage but dispensable for cleavage of other death substrates in apoptosis. J. Biol. Chem. 273, 15540–15545 (1998).
  Article CAS Google Scholar
• Laster, S. M. & Mackenzie, J. M. Jr Bleb formation and F-actin distribution during mitosis and tumor necrosis factor-induced apoptosis. Microsc. Res. Tech. 34, 272–280 (1996).
  Article CAS Google Scholar
• Mills, J. C., Stone, N. L., Erhardt, J. & Pittman, R. N. Apoptotic membrane blebbing is regulated by myosin light chain phosphorylation. J. Cell. Biol. 140, 627–636 (1998).
  Article CAS Google Scholar
• Huot, J. et al. SAPK2/p38-dependent F-actin reorganization regulates early membrane blebbing during stress-induced apoptosis. J. Cell. Biol. 143, 1361–1373 (1998).
  Article CAS Google Scholar
• Mills, J. C., Stone, N. L. & Pittman, R. N. Extranuclear apoptosis. The role of the cytoplasm in the execution phase. J. Cell. Biol. 146, 703–708 (1999).
  Article CAS Google Scholar
• Kohama, K., Ye, L. H., Hayakawa, K. & Okagaki, T. Myosin light chain kinase: an actin-binding protein that regulates an ATP-dependent interaction with myosin. Trends Pharmacol. Sci. 17, 284–287 (1996).
  Article CAS Google Scholar
• Alessi, D., MacDougall, L. K., Sola, M. M., Ikebe, M. & Cohen, P. The control of protein phosphatase-1 by targetting subunits. The major myosin phosphatase in avian smooth muscle is a novel form of protein phosphatase-1. Eur. J. Biochem. 210, 1023–1035 (1992).
  Article CAS Google Scholar
• Amano, M. et al. Phosphorylation and activation of myosin by Rho-associated kinase (Rho–kinase). J. Biol. Chem. 271, 20246–20249 (1996).
  Article CAS Google Scholar
• Kimura, K. et al. Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rho–kinase). Science 273, 245–248 (1996).
  Article CAS Google Scholar
• Kawano, Y. et al. Phosphorylation of myosin-binding subunit (MBS) of myosin phosphatase by Rho–kinase in vivo. J. Cell. Biol. 147, 1023–1038 (1999).
  Article CAS Google Scholar
• Ishizaki, T. et al. 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 (1996).
  Article CAS Google Scholar
• Leung, T., Manser, E., Tan, L. & Lim, L. A novel serine/threonine kinase binding the Ras-related RhoA GTPase which translocates the kinase to peripheral membranes. J. Biol. Chem. 270, 29051–29054 (1995).
  Article CAS Google Scholar
• Leung, T., Chen, X. Q., Manser, E. & Lim, L. The p160 RhoA-binding kinase ROK alpha is a member of a kinase family and is involved in the reorganization of the cytoskeleton. Mol. Cell. Biol. 16, 5313–5327 (1996).
  Article CAS Google Scholar
• Janicke, R. U., Sprengart, M. L., Wati, M. R. & Porter, A. G. Caspase-3 is required for DNA fragmentation and morphological changes associated with apoptosis. J. Biol. Chem. 273, 9357–9360 (1998).
  Article CAS Google Scholar
• Scaffidi, C., Krammer, P. H. & Peter, M. E. Isolation and analysis of components of CD95 (APO-1/Fas) death-inducing signaling complex. Methods 17, 287–291 (1999).
  Article CAS Google Scholar
• Ishizaki, T. et al. p160ROCK, a Rho-associated coiled-coil forming protein kinase, works downstream of Rho and induces focal adhesions. FEBS Lett. 404, 118–124 (1997).
  Article CAS Google Scholar
• Uehata, M. et al. Calcium sensitization of smooth muscle mediated by a Rho-associated protein kinase in hypertension. Nature 389, 990–994 (1997).
  Article CAS Google Scholar
• Itoh, K. et al. An essential part for Rho-associated kinase in the transcellular invasion of tumor cells. Nature Med. 5, 221–225 (1999).
  Article CAS Google Scholar
• Klages, B., Brandt, U., Simon, M. I., Schultz, G. & Offermanns, S. Activation of G12/G13 results in shape change and Rho/Rho–kinase-mediated myosin light chain phosphorylation in mouse platelets. J. Cell. Biol. 144, 745–754 (1999).
  Article CAS Google Scholar
• Essler, M., Staddon, J. M., Weber, P. C. & Aepfelbacher, M. Cyclic AMP blocks bacterial lipopolysaccharide-induced myosin light chain phosphorylation in endothelial cells through inhibition of Rho/Rho kinase signaling. J. Immunol. 164, 6543–6549 (2000).
  Article CAS Google Scholar
• Ishizaki, T. et al. Pharmacological properties of Y-27632, a specific inhibitor of rho-associated kinases. Mol. Pharmacol. 57, 976–983 (2000).
  CAS Google Scholar
• Sekine, A., Fujiwara, M. & Narumiya, S. Asparagine residue in the rho gene product is the modification site for botulinum ADP–ribosyltransferase. J. Biol. Chem. 264, 8602–8605 (1989).
  CAS Google Scholar
• 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, 389–399 (1992).
  Article CAS Google Scholar
• Nagahara, H. et al. Transduction of full-length TAT fusion proteins into mammalian cells: TAT-p27Kip1 induces cell migration. Nature Med. 4, 1449–1452 (1998).
  Article CAS Google Scholar
• Hirose, M. et al. Molecular dissection of the Rho-associated protein kinase (p160ROCK)-regulated neurite remodeling in neuroblastoma N1E-115 cells. J. Cell. Biol. 141, 1625–1636 (1998).
  Article CAS Google Scholar
• Hall, A. Rho GTPases and the actin cytoskeleton. Science 279, 509–514 (1998).
  Article CAS Google Scholar
• McCarthy, N. J., Whyte, M. K., Gilbert, C. S. & Evan, G. I. Inhibition of Ced-3/ICE-related proteases does not prevent cell death induced by oncogenes, DNA damage, or the Bcl-2 homologue Bak. J. Cell. Biol. 136, 215–227 (1997).
  Article CAS Google Scholar
• Katoh, H. et al. Constitutively active α12, Gα13, and Gαq induce Rho-dependent neurite retraction through different signaling pathways. J. Biol. Chem. 273, 28700–28707 (1998).
  Article CAS Google Scholar
• Rao, J. Y. et al. Alterations of the actin polymerization status as an apoptotic morphological effector in HL-60 cells. J. Cell Biochem. 75, 686–697 (1999).
  Article CAS Google Scholar
• Ohashi, K. et al. Rho-associated kinase ROCK activates LIM-kinase 1 by phosphorylation at threonine 508 within the activation loop. J. Biol. Chem. 275, 3577–35782 (2000).
  Article CAS Google Scholar
• Ratcliffe, M. J., Smales, C. & Staddon, J. M. Dephosphorylation of the catenins p120 and p100 in endothelial cells in response to inflammatory stimuli. Biochem. J. 338, 471–478 (1999).
  Article CAS Google Scholar
• Zapata, J. M., Takahashi, R., Salvesen, G. S. & Reed, J. C. Granzyme release and caspase activation in activated human T-lymphocytes. J. Biol. Chem. 273, 6916–6920 (1998).
  Article CAS Google Scholar
• Chardin, P. et al. The mammalian G protein rhoC is ADP-ribosylated by Clostridium botulinum exoenzyme C3 and affects actin microfilaments in Vero cells. EMBO J. 8, 1087–1092 (1989).
  Article CAS Google Scholar
• Lang, P. et al. Characterization of a monoclonal antibody specific for the Ras-related GTP-binding protein Rho A. Biochem. Biophys. Res. Commun. 196, 1522–1528 (1993).
  Article CAS Google Scholar