Overexpression of Kinase Suppressor of Ras Upregulates the High-Molecular-Weight Tropomyosin Isoforms in ras-Transformed NIH 3T3 Fibroblasts

REFERENCES

• Alaiya, A. A., B. Franzen, K. Fujioka, B. Moberger, K. Schedvins, C. Silfversvard, S. Linder, and G. Auer. 1997. Phenotypic analysis of ovarian carcinoma: polypeptide expression in benign, borderline and malignant tumors. Int. J. Cancer 73: 678–683.
   PubMed Web of Science ®Google Scholar
• Alaiya, A. A., M. Oppermann, J. Langridge, U. Roblick, L. Egevad, S. Brindstedt, M. Hellstrom, S. Linder, T. Bergman, H. Jornvall, and G. Auer. 2001. Identification of proteins in human prostate tumor material by two-dimensional gel electrophoresis and mass spectrometry. Cell. Mol. Life Sci. 58: 307–311.
   PubMed Web of Science ®Google Scholar
• Amano, M., M. Ito, K. Kimura, Y. Fukata, K. Chihara, T. Nakano, Y. Matsuura, and K. Kaibuchi. 1996. Phosphorylation and activation of myosin by Rho-associated kinase (Rho-kinase). J. Biol. Chem. 271: 20246–20249.
   PubMed Web of Science ®Google Scholar
• Anselmo, A. N., R. Bumeister, J. M. Thomas, and M. A. White. 2002. Critical contribution of linker proteins to raf kinase activation. J. Biol. Chem. 277: 5940–5943.
   PubMedGoogle Scholar
• Behre, G., L. T. Smith, and D. G. Tenen. 1999. Use of a promoterless Renilla luciferase vector as an internal control plasmid for transient co-transfection assays of Ras-mediated transcription activation. BioTechniques 26: 24–26, 28.
   PubMedGoogle Scholar
• Bell, B., H. Xing, K. Yan, N. Gautam, and A. J. Muslin. 1999. KSR-1 binds to G-protein beta gamma subunits and inhibits beta gamma-induced mitogen-activated protein kinase activation. J. Biol. Chem. 274: 7982–7986.
   PubMedGoogle Scholar
• Bhattacharya, B., G. L. Prasad, E. M. Valverius, D. S. Salomon, and H. L. Cooper. 1990. Tropomyosins of human mammary epithelial cells: consistent defects of expression in mammary carcinoma cell lines. Cancer Res. 50: 2105–2112.
   PubMedGoogle Scholar
• Boyd, J., J. I. Risinger, R. W. Wiseman, B. A. Merrick, J. K. Selkirk, and J. C. Barrett. 1996. Regulation of microfilament organization and anchorage-independent growth by tropomyosin 1. Proc. Natl. Acad. Sci. USA 92: 11534–11538.
   Google Scholar
• Brennan, J. A., D. J. Volle, O. V. Chaika, and R. E. Lewis. 2002. Phosphorylation regulates the nucleocytoplasmic distribution of kinase suppressor of Ras. J. Biol. Chem. 277: 5369–5377.
   PubMed Web of Science ®Google Scholar
• Cacace, A. M., N. R. Michaud, M. Therrien, K. Mathes, T. Copeland, G. M. Rubin, and D. K. Morrison. 1999. Identification of constitutive and Ras-inducible phosphorylation sites of KSR: implications for 14-3-3 binding, mitogen-activated protein kinase binding, and KSR overexpression. Mol. Cell. Biol. 19: 229–240.
   PubMed Web of Science ®Google Scholar
• Cooper, H. L., B. Bhattacharya, R. H. Bassin, and D. S. Salomon. 1987. Suppression of synthesis and utilization of tropomyosin in mouse and rat fibroblasts by transforming growth factor alpha: a pathway in oncogene action. Cancer Res. 47: 4493–4500.
   PubMedGoogle Scholar
• Denouel-Galy, A., E. M. Douville, P. H. Warne, C. Papin, D. Laugier, G. Calothy, J. Downward, and A. Eychene. 1998. Murine Ksr interacts with MEK and inhibits Ras-induced transformation. Curr. Biol. 8: 46–55.
   PubMed Web of Science ®Google Scholar
• Franzen, B., S. Linder, A. A. Alaiya, E. Eriksson, K. Fujioka, A. C. Bergman, H. Jornvall, and G. Auer. 1997. Analysis of polypeptide expression in benign and malignant human breast lesions. Electrophoresis 18: 582–587.
   PubMed Web of Science ®Google Scholar
• Franzen, B., S. Linder, K. Uryu, A. A. Alaiya, T. Hirano, H. Kato, and G. Auer. 1996. Expression of tropomyosin isoforms in benign and malignant human breast lesions. Br. J. Cancer 73: 909–913.
   PubMed Web of Science ®Google Scholar
• Gimona, M., J. A. Kazzaz, and D. M. Helfman. 1996. Forced expression of tropomyosin 2 or 3 in v-Ki-ras-transformed fibroblasts results in distinct phenotypic effects. Proc. Natl. Acad. Sci. USA 93: 9618–9623.
   PubMedGoogle Scholar
• Goodwin, L. O., J. P. Lees-Miller, M. A. Leonard, S. B. Cheley, and D. M. Helfman. 1991. Four fibroblast tropomyosin isoforms are expressed from the rat alpha-tropomyosin gene via alternative RNA splicing and the use of two promoters. J. Biol. Chem. 266: 8408–8415.
   PubMedGoogle Scholar
• He, T. C., S. Zhou, L. T. da Costa, J. Yu, K. W. Kinzler, and B. Vogelstein. 1998. A simplified system for generating recombinant adenoviruses. Proc. Natl. Acad. Sci. USA 95: 2509–2514.
   PubMed Web of Science ®Google Scholar
• Helfman, D. M., S. Cheley, E. Kuismanen, L. A. Finn, and Y. Yamawaki-Kataoka. 1986. Nonmuscle and muscle tropomyosin isoforms are expressed from a single gene by alternative RNA splicing and polyadenylation. Mol. Cell. Biol. 6: 3582–3595.
   PubMed Web of Science ®Google Scholar
• Hendricks, M., and H. Weintraub. 1981. Tropomyosin is decreased in transformed cells. Proc. Natl. Acad. Sci. USA 78: 5633–5637.
   PubMedGoogle Scholar
• Herrera, V. L., and N. Ruiz-Opazo. 1990. Regulation of alpha-tropomyosin and N5 genes by a shared enhancer. Modular structure and hierarchical organization. J. Biol. Chem. 265: 9555–9562.
   PubMedGoogle Scholar
• Huang, A. M., and G. M. Rubin. 2000. A misexpression screen identifies genes that can modulate RAS1 pathway signaling in Drosophila melanogaster. Genetics 156: 1219–1230.
   PubMed Web of Science ®Google Scholar
• Janssen, R. A., and J. W. Mier. 1997. Tropomyosin-2 cDNA lacking the 3′ untranslated region riboregulator induces growth inhibition of v-Ki-ras-transformed fibroblasts. Mol. Biol. Cell 8: 897–908.
   PubMedGoogle Scholar
• Janssen, R. A., K. G. Veenstra, P. Jonasch, E. Jonasch, and J. W. Mier. 1998. Ras- and Raf-induced down-modulation of non-muscle tropomyosin are MEK-independent. J. Biol. Chem. 273: 32182–32186.
   PubMed Web of Science ®Google Scholar
• Joneson, T., J. A. Fulton, D. J. Volle, O. V. Chaika, D. Bar-Sagi, and R. E. Lewis. 1998. Kinase suppressor of Ras inhibits the activation of extracellular ligand-regulated (ERK) mitogen-activated protein (MAP) kinase by growth factors, activated Ras, and Ras effectors. J. Biol. Chem. 273: 7743–7748.
   PubMed Web of Science ®Google Scholar
• Kim, P. N., E. Jonasch, B. C. Mosterman, J. W. Mier, and R. A. J. Janssen. 2001. Radicicol suppresses transformation and restores tropomyosin-2 expression in both ras- and MEK-transformed cells without inhibiting the Raf/MEK/ERK signaling cascade. Cell Growth Differ. 12: 543–550.
   PubMedGoogle Scholar
• 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 273: 245–248.
   PubMed Web of Science ®Google Scholar
• Lee, S. W., C. Tomasetto, and R. Sager. 1991. Positive selection of candidate tumor-suppressor genes by subtractive hybridization. Proc. Natl. Acad. Sci. USA 88: 2825–2829.
   PubMed Web of Science ®Google Scholar
• Lees-Miller, J. P., L. O. Goodwin, and D. M. Helfman. 1990. Three novel brain tropomyosin isoforms are expressed from the rat α-tropomyosin gene through the use of alternative promoters and alternative RNA processing. Mol. Cell. Biol. 10: 1729–1742.
   PubMed Web of Science ®Google Scholar
• Lees-Miller, J. P., and D. M. Helfman. 1991. The molecular basis for tropomyosin isoform diversity. BioEssays 13: 429–437.
   PubMedGoogle Scholar
• Levchenko, A., J. Bruck, and P. W. Sternberg. 2000. Scaffold proteins may biphasically affect the levels of mitogen-activated protein kinase signaling and reduce its threshold properties. Proc. Natl. Acad. Sci. USA 97: 5818–5823.
   PubMed Web of Science ®Google Scholar
• Ljungdahl, S., S. Linder, B. Franzen, B. Binetruy, G. Auer, and M. C. Shoshan. 1998. Down-regulation of tropomyosin-2 expression in c-Jun-transformed rat fibroblasts involves induction of a MEK1-dependent autocrine loop. Cell Growth Differ. 9: 565–573.
   PubMedGoogle Scholar
• Maekawa, M., T. Ishizaki, S. Boku, N. Watanabe, A. Fujita, A. Iwamatsu, T. Obinata, K. Ohashi, K. Mizuno, and S. Narumiya. 1999. Signaling from Rho to the actin cytoskeleton through protein kinases ROCK and LIM-kinase. Science 285: 895–898.
   PubMed Web of Science ®Google Scholar
• Matsumura, F., J. J. Lin, S. Yamashiro-Matsumura, G. P. Thomas, and W. C. Topp. 1983. Differential expression of tropomyosin forms in the microfilaments isolated from normal and transformed rat cultured cells. J. Biol. Chem. 258: 13954–13964.
   PubMedGoogle Scholar
• Matsumura, F., S. Ono, Y. Yamakita, G. Totsukawa, and S. Yamashiro. 1998. Specific localization of serine 19 phosphorylated myosin II during cell locomotion and mitosis of cultured cells. J. Cell Biol. 140: 119–129.
   PubMedGoogle Scholar
• Morrison, D. K. 2001. KSR: a MAPK scaffold of the Ras pathway? J. Cell Sci. 114: 1609–1612.
   PubMed Web of Science ®Google Scholar
• Müller, J., A. M. Cacace, W. E. Lyons, C. B. McGill, and D. K. Morrison. 2000. Identification of B-KSR1, a novel brain-specific isoform of KSR1 that functions in neuronal signaling. Mol. Cell. Biol. 20: 5529–5539.
   PubMed Web of Science ®Google Scholar
• Müller, J., S. Ory, T. Copeland, H. Piwnica-Worms, and D. K. Morrison. 2001. C-TAK1 regulates Ras signaling by phosphorylating the MAPK scaffold, KSR1. Mol. Cell 8: 983–993.
   PubMed Web of Science ®Google Scholar
• Nguyen, A., W. R. Burack, J. L. Stock, R. Kortum, O. V. Chaika, M. Afkarian, W. J. Muller, K. M. Murphy, D. K. Morrison, R. E. Lewis, J. McNeish, and A. S. Shaw. 2002. Kinase suppressor of Ras (KSR) is a scaffold which facilitates mitogen-activated protein kinase activation in vivo. Mol. Cell. Biol. 22: 3035–3045.
   PubMed Web of Science ®Google Scholar
• Pawlak, G., and D. M. Helfman. 2001. Cytoskeletal changes in cell transformation and tumorigenesis. Curr. Opin. Genet. Dev. 11: 41–47.
   PubMed Web of Science ®Google Scholar
• Pawlak, G., and D. M. Helfman. 2002. Post-transcriptional down-regulation of ROCKI/Rho-kinase through an MEK-dependent pathway leads to cytoskeleton disruption in Ras-transformed fibroblasts. Mol. Biol. Cell 13: 336–347.
   PubMedGoogle Scholar
• Percival, J. M., G. Thomas, T. A. Cock, E. M. Gardiner, P. L. Jeffrey, J. J. Lin, R. P. Weinberger, and P. Gunning. 2000. Sorting of tropomyosin isoforms in synchronised NIH 3T3 fibroblasts: evidence for distinct microfilament populations. Cell Motil. Cytoskel. 47: 189–208.
   PubMedGoogle Scholar
• Perry, R. L., M. H. Parker, and M. A. Rudnicki. 2001. Activated MEK1 binds the nuclear MyoD transcriptional complex to repress transactivation. Mol. Cell 8: 291–301.
   PubMed Web of Science ®Google Scholar
• Pittenger, M. F., J. A. Kazzaz, and D. M. Helfman. 1994. Functional properties of non-muscle tropomyosin isoforms. Curr. Opin. Cell Biol. 6: 96–104.
   PubMed Web of Science ®Google Scholar
• Prasad, G. L., R. A. Fuldner, and H. L. Cooper. 1993. Expression of transduced tropomyosin 1 cDNA suppresses neoplastic growth of cells transformed by the ras oncogene. Proc. Natl. Acad. Sci. USA 90: 7039–7043.
   PubMed Web of Science ®Google Scholar
• Prasad, G. L., L. Masuelli, M. H. Raj, and N. Harindranath. 1999. Suppression of src-induced transformed phenotype by expression of tropomyosin-1. Oncogene 18: 2027–2031.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Ridley, A. J., and A. Hall. 1994. Signal transduction pathways regulating Rho-mediated stress fibre formation: requirement for a tyrosine kinase. EMBO J. 13: 2600–2610.
   PubMed Web of Science ®Google Scholar
• Roy, F., G. Laberge, M. Douziech, D. Ferland-McCollough, and M. Therrien. 2002. KSR is a scaffold required for activation of the ERK/MAPK module. Genes Dev. 16: 427–438.
   PubMed Web of Science ®Google Scholar
• Sahai, E., A. S. Alberts, and R. Treisman. 1998. RhoA effector mutants reveal distinct effector pathways for cytoskeletal reorganization, SRF activation and transformation. EMBO J. 17: 1350–1361.
   PubMed Web of Science ®Google Scholar
• Sahai, E., M. F. Olson, and C. J. Marshall. 2001. Cross-talk between Ras and Rho signalling pathways in transformation favours proliferation and increased motility. EMBO J. 20: 755–766.
   PubMed Web of Science ®Google Scholar
• Seddighzadeh, M., S. Linder, M. C. Shoshan, G. Auer, and A. A. Alaiya. 2000. Inhibition of extracellular signal-regulated kinase 1/2 activity of the breast cancer cell line MDA-MB-231 leads to major alterations in the pattern of protein expression. Electrophoresis 21: 2737–2743.
   PubMedGoogle Scholar
• Shah, V., S. Bharadwaj, K. Kaibuchi, and G. L. Prasad. 2001. Cytoskeletal organization in tropomyosin-mediated reversion of ras-transformation: evidence for Rho kinase pathway. Oncogene 20: 2112–2121.
   PubMedGoogle Scholar
• Shields, J. M., H. Mehta, K. Pruitt, and C. J. Der. 2002. Opposing roles of the extracellular signal-regulated kinase and p38 mitogen-activated protein kinase cascades in Ras-mediated downregulation of tropomyosin. Mol. Cell. Biol. 22: 2304–2317.
   PubMed Web of Science ®Google Scholar
• Stamm, S., D. Casper, J. P. Lees-Miller, and D. M. Helfman. 1993. Brain-specific tropomyosins TMBr-1 and TMBr-3 have distinct patterns of expression during development and in adult brain. Proc. Natl. Acad. Sci. USA 90: 9857–9861.
   PubMed Web of Science ®Google Scholar
• Sternberg, P. W., and J. Alberola-Ila. 1998. Conspiracy theory: RAS and RAF do not act alone. Cell 95: 447–450.
   PubMedGoogle Scholar
• Stewart, S., M. Sundaram, Y. Zhang, J. Lee, M. Han, and K.-L. Guan. 1999. Kinase suppressor of Ras forms a multiprotein signaling complex and modulates MEK localization. Mol. Cell. Biol. 19: 5523–5534.
   PubMed Web of Science ®Google Scholar
• Sugimoto, T., S. Stewart, M. Han, and K. L. Guan. 1998. The kinase suppressor of Ras (KSR) modulates growth factor and Ras signaling by uncoupling Elk-1 phosphorylation from MAP kinase activation. EMBO J. 17: 1717–1727.
   PubMed Web of Science ®Google Scholar
• Sumi, T., K. Matsumoto, and T. Nakamura. 2000. Specific activation of LIM kinase 2 via phosphorylation of threonine 505 by ROCK, a Rho-dependent protein kinase. J. Biol. Chem. 276: 670–676.
   Google Scholar
• Sundaram, M., and M. Han. 1995. The C. elegans ksr-1 gene encodes a novel Raf-related kinase involved in Ras-mediated signal transduction. Cell 83: 889–901.
   PubMed Web of Science ®Google Scholar
• Takenaga, K., and A. Masuda. 1994. Restoration of microfilament bundle organization in v-raf-transformed NRK cells after transduction with tropomyosin 2 cDNA. Cancer Lett. 87: 47–53.
   PubMedGoogle Scholar
• Therrien, M., H. C. Chang, N. M. Solomon, F. D. Karim, D. A. Wassarman, and G. M. Rubin. 1995. KSR, a novel protein kinase required for RAS signal transduction. Cell 83: 879–888.
   PubMed Web of Science ®Google Scholar
• Totsukawa, G., Y. Yamakita, S. Yamashiro, D. J. Hartshorne, Y. Sasaki, and F. Matsumura. 2000. Distinct roles of ROCK (Rho-kinase) and MLCK in spatial regulation of MLC phosphorylation for assembly of stress fibers and focal adhesions in 3T3 fibroblasts. J. Cell Biol. 150: 797–806.
   PubMed Web of Science ®Google Scholar
• Xing, H., K. Kornfeld, and A. J. Muslin. 1997. The protein kinase KSR interacts with 14-3-3 protein and Raf. Curr. Biol. 7: 294–300.
   PubMedGoogle Scholar
• Yang, N., O. Higuchi, K. Ohashi, K. Nagata, A. Wada, K. Kangawa, E. Nishida, and K. Mizuno. 1998. Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization. Nature 393: 809–812.
   PubMed Web of Science ®Google Scholar
• Yu, W., W. J. Fantl, G. Harrowe, and L. T. Williams. 1998. Regulation of the MAP kinase pathway by mammalian Ksr through direct interaction with MEK and ERK. Curr. Biol. 8: 56–64.
   PubMed Web of Science ®Google Scholar
• Zhou, M., D. A. Horita, D. S. Waugh, R. A. Byrd, and D. K. Morrison. 2002. Solution structure and functional analysis of the cysteine-rich C1 domain of kinase suppressor of Ras (KSR). J. Mol. Biol. 315: 435–446.
   PubMed Web of Science ®Google Scholar