SSeCKS, a Major Protein Kinase C Substrate with Tumor Suppressor Activity, Regulates G₁→S Progression by Controlling the Expression and Cellular Compartmentalization of Cyclin D

REFERENCES

• Assoian, R. K.. 1997. Anchorage-dependent cell cycle progression. J. Cell Biol. 136:1–4
   PubMed Web of Science ®Google Scholar
• Baldin, V., Lukas, J., Marcote, M. J., Pagano, M., and Draetta, G.. 1993. Cyclin D1 is a nuclear protein required for cell cycle progression in G1. Genes Dev. 7:812–821
   PubMed Web of Science ®Google Scholar
• Brancolini, C., and Schneider, C.. 1994. Phosphorylation of the growth arrest-specific protein Gas2 is coupled to actin rearrangements during G0→G1 transition in NIH 3T3 cells. J. Cell Biol. 124:743–756
   PubMedGoogle Scholar
• Brugarolas, J., Bronson, R. T., and Jacks, T.. 1998. p21 is a critical CDK2 regulator essential for proliferation control in Rb-deficient cells. J. Cell Biol. 141:503–514
   PubMedGoogle Scholar
• Brugarolas, J., Chandrasekaran, C., Gordon, J. I., Beach, D., Jacks, T., and Hannon, G. J.. 1995. Radiation-induced cell cycle arrest compromised by p21 deficiency. Nature 377:552–557
   PubMed Web of Science ®Google Scholar
• Burridge, K., and Chrzanowska-Wodnicka, M.. 1996. Focal adhesions, contractility, and signaling. Annu. Rev. Cell Biol. 12:463–518
   Google Scholar
• Burridge, K.. 1999. Signal transduction—crosstalk between Rac and Rho. Science 283:2028–2029
   PubMedGoogle Scholar
• Chapline, C., Cottom, J., Tobin, H., Hulmes, J., Crabb, J., and Jaken, S.. 1998. A major, transformation-sensitive PKC-binding protein is also a PKC substrate involved in cytoskeletal remodeling. J. Biol. Chem. 273:19482–19489
   PubMed Web of Science ®Google Scholar
• Chapline, C., Mousseau, B., Ramsay, K., Duddy, S., Li, Y., Kiley, S. C., and Jaken, S.. 1996. Identification of a major protein kinase C-binding protein and substrate in rat embryo fibroblasts—decreased expression in transformed cells. J. Biol. Chem. 271:6417–6422
   PubMed Web of Science ®Google Scholar
• Chen, J., Saha, P., Kornbluth, S., Dynlacht, B. D., and Dutta, A.. 1996. Cyclin-binding motifs are essential for the function of p21CIP1. Mol. Cell. Biol. 16:4673–4682
   PubMed Web of Science ®Google Scholar
• Chen, Y., Farmer, A. A., Chen, C. F., Jones, D. C., Chen, P. L., and Lee, W. H.. 1996. BRCA1 is a 220-kDa nuclear phosphoprotein that is expressed and phosphorylated in a cell cycle-dependent manner. Cancer Res. 56:3168–3172 (Erratum, 56:4074.)
   PubMed Web of Science ®Google Scholar
• Cheng, M., Olivier, P., Diehl, J. A., Fero, M., Roussel, M. F., Roberts, J. M., and Sherr, C. J.. 1999. The p21(Cip1) and p27(Kip1) CDK ‘inhibitors’ are essential activators of cyclin D-dependent kinases in murine fibroblasts. EMBO J. 18:1571–1583
   PubMed Web of Science ®Google Scholar
• Chow, M., and Rubin, H.. 1996. Evidence for cellular aging in long-term confluent cultures: heritable impairment of proliferation, accumulation of age pigments and their loss in neoplastic transformation. Mech. Ageing Dev. 89:165–183
   PubMed Web of Science ®Google Scholar
• Chow, M., and Rubin, H.. 1996. Irreversibility of cellular aging and neoplastic transformation: a clonal analysis. Proc. Natl. Acad. Sci. USA 93:9793–9798
   PubMedGoogle Scholar
• Daduang, S., Kimura, K., Nagata, S., and Fukui, Y.. 1998. Density dependent elevation of phosphatidylinositol-3 kinase level in rat 3Y1 cells. Biochim. Biophys. Acta 1401:113–120
   PubMedGoogle Scholar
• DelSal, G., Loda, M., and Pagano, M.. 1996. Cell cycle and cancer: critical events at the G1 restriction point. Crit. Rev. Oncol. 7:127–142
   Google Scholar
• Derossi, D., Chassaing, G., and Prochiantz, A.. 1998. Trojan peptides: the penetratin system for intracellular delivery. Trends Cell. Biol. 8:84–87
   PubMed Web of Science ®Google Scholar
• Derossi, D., Joliot, A. H., Chassaing, G., and Prochiantz, A.. 1994. The third helix of the Antennapedia homeodomain translocates through biological membranes. J. Biol. Chem. 269:10444–10450
   PubMed Web of Science ®Google Scholar
• Diehl, J. A., Cheng, M., Roussel, M. F., and Sherr, C. J.. 1998. Glycogen synthase kinase-3β regulates cyclin D1 proteolysis and subcellular localization. Genes Dev. 12:3499–3511
   PubMed Web of Science ®Google Scholar
• Diehl, J. A., and Sherr, C. J.. 1997. A dominant-negative cyclin D1 mutant prevents nuclear import of cyclin-dependent kinase 4 (CDK4) and its phosphorylation by CDK-activating kinase. Mol. Cell. Biol. 17:7362–7374
   PubMed Web of Science ®Google Scholar
• Diehl, J. A., Zindy, F., and Sherr, C. J.. 1997. Inhibition of cyclin D1 phosphorylation on threonine-286 prevents its rapid degradation via the ubiquitin-proteasome pathway. Genes Dev. 11:957–972
   PubMed Web of Science ®Google Scholar
• Dietrich, C., Wallenfang, K., Oesch, F., and Wieser, R.. 1997. Translocation of cdk2 to the nucleus during G1-phase in PDGF-stimulated human fibroblasts. Exp. Cell Res. 232:72–78
   PubMedGoogle Scholar
• Faux, M. C., and Scott, J. D.. 1996. Molecular glue: kinase anchoring and scaffold proteins. Cell 85:9–12
   PubMedGoogle Scholar
• Gelman, I., Khan, S., and Hanafusa, H.. 1993. Morphological transformation, tumorigenicity and src-specific cytotoxic T lymphocyte-mediated tumor immunity induced by murine 3T3 cells expressing src oncogenes encoding novel non-myristylated N-terminal domains. Oncogene 8:2995–3004
   PubMedGoogle Scholar
• Gelman, I. H., Lee, K., Tombler, E., Gordon, R., and Lin, X.. 1998. Control of cytoskeletal architecture by the src-suppressed C kinase substrate, SSeCKS. Cell Motil. Cytoskeleton 41:1–17
   PubMed Web of Science ®Google Scholar
• Geng, Y., Whoriskey, W., Park, M. Y., Bronson, R. T., Medema, R. H., Li, T., Weinberg, R. A., and Sicinski, P.. 1999. Rescue of cyclin D1 deficiency by knockin cyclin E. Cell 97:767–777
   PubMed Web of Science ®Google Scholar
• Gossen, M., Bonin, A. L., and Bujard, H.. 1993. Control of gene activity in higher eukaryotic cells by prokaryotic regulatory elements. Trends Biochem. Sci. 18:471–475
   PubMed Web of Science ®Google Scholar
• Gossen, M., and Bujard, H.. 1992. Tight control of gene expression in mammalian cells by tetracycline-responsive promoters. Proc. Natl. Acad. Sci. USA 89:5547–5551
   PubMed Web of Science ®Google Scholar
• Gradl, G., Faust, D., Oesch, F., and Wieser, R. J.. 1995. Density-dependent regulation of cell growth by contactinhibin and the contactinhibin receptor. Curr. Biol. 5:526–535
   PubMedGoogle Scholar
• Gustincich, S., and Schneider, C.. 1993. Serum deprivation response gene is induced by serum starvation but not by contact inhibition. Cell Growth Differ. 4:753–760
   PubMedGoogle Scholar
• Hinds, P. W., Mittnacht, S., Dulic, V., Arnold, A., Reed, S. I., and Weinberg, R. A.. 1992. Regulation of retinoblastoma protein functions by ectopic expression of human cyclins. Cell 70:993–1006
   PubMed Web of Science ®Google Scholar
• Hochholdinger, F., Baier, G., Nogalo, A., Bauer, B., Grunicke, H. H., and Uberall, F.. 1999. Novel membrane-targeted ERK1 and ERK2 chimeras which act as dominant negative, isotype-specific mitogen-activated protein kinase inhibitors of Ras-Raf-mediated transcriptional activation of c-fos in NIH 3T3 cells. Mol. Cell. Biol. 19:8052–8065
   PubMedGoogle Scholar
• Ingber, D. E.. 1997. Tensegrity: the architectural basis of cellular mechanotransduction. Annu. Rev. Physiol. 59:575–599
   PubMed Web of Science ®Google Scholar
• Kaplan, M. H., Daniel, C., Schindler, U., and Grusby, M. J.. 1998. Stat proteins control lymphocyte proliferation by regulating p27Kip1 expression. Mol. Cell. Biol. 18:1996–2003
   PubMed Web of Science ®Google Scholar
• Kato, A., Takahashi, H., Takahashi, Y., and Matsushime, H.. 1997. Inactivation of the cyclin D-dependent kinase in the rat fibroblast cell line, 3Y1, induced by contact inhibition. J. Biol. Chem. 272:8065–8070
   PubMedGoogle Scholar
• Knudsen, E. S., and Wang, J. Y.. 1997. Dual mechanisms for the inhibition of E2F binding to RB by cyclin-dependent kinase-mediated RB phosphorylation. Mol. Cell. Biol. 17:5771–5783
   PubMed Web of Science ®Google Scholar
• Lavoie, J. N., Rivard, N., L'Allemain, G., and Pouyssegur, J.. 1996. A temporal and biochemical link between growth factor-activated MAP kinases, cyclin D1 induction and cell cycle entry. Prog. Cell Cycle Res. 2:49–58
   PubMedGoogle Scholar
• Lin, X., and Gelman, I. H.. 1997. Re-expression of the major protein kinase C substrate, SSeCKS, suppresses v-src-induced morphological transformation and tumorigenesis. Cancer Res. 57:2304–2312
   PubMed Web of Science ®Google Scholar
• Lin, X., Nelson, P. J., Frankfort, B., Tombler, E., Johnson, R., and Gelman, I. H.. 1995. Isolation and characterization of a novel mitogenic regulatory gene, 322, which is transcriptionally suppressed in cells transformed by src and ras. Mol. Cell. Biol. 15:2754–2762
   PubMed Web of Science ®Google Scholar
• Lin, X., Tombler, E., Nelson, P. J., Ross, M., and Gelman, I. H.. 1996. A novel src- and ras-suppressed protein kinase C substrate associated with cytoskeletal architecture. J. Biol. Chem. 271:28430–28438
   PubMedGoogle Scholar
• Nakayama, K., Ishida, N., Shirane, M., Inomata, A., Inoue, T., Shishido, N., Horii, I., and Loh, D. Y.. 1996. Mice lacking p27(Kip1) display increased body size, multiple organ hyperplasia, retinal dysplasia, and pituitary tumors. Cell 85:707–720
   PubMed Web of Science ®Google Scholar
• Nauert, J., Klauck, T., Langeberg, L. K., and Scott, J. D.. 1997. Gravin, an autoantigen recognized by serum from myasthenia gravis patients, is a kinase scaffolding protein. Curr. Biol. 7:52–62
   PubMed Web of Science ®Google Scholar
• Nelson, P., and Gelman, I. H.. 1997. Cell-cycle regulated expression and serine phosphorylation of the myristylated protein kinase C substrate, SSeCKS: correlation with cell confluency, G0 phase and serum response. Mol. Cell. Biochem. 175:233–241
   PubMedGoogle Scholar
• Nelson, P. J., Moissoglu, K., Vargas, J. J., Klotman, P. E., and Gelman, I. H.. 1999. Involvement of the protein kinase C substrate, SSeCKS, in the actin-based stellate morphology of mesangial cells. J. Cell Sci. 112:361–370
   PubMed Web of Science ®Google Scholar
• Norton, K. K., Mahadeo, D. K., Geist, R. T., and Gutmann, D. H.. 1996. Expression of the neurofibromatosis 1 (NF1) gene during growth arrest. Neuroreport 7:601–604
   PubMedGoogle Scholar
• Pawson, T., and Scott, J. D.. 1997. Signaling through scaffold, anchoring, and adaptor proteins. Science 278:2075–2080
   PubMed Web of Science ®Google Scholar
• Peck, D., and Isacke, C. M.. 1998. Hyaluronan-dependent cell migration can be blocked by a CD44 cytoplasmic domain peptide containing a phosphoserine at position 325. J. Cell Sci. 111:1595–1601
   PubMedGoogle Scholar
• Pines, J.. 1995. Cell cycle. Conformational change. Nature 376:294–295
   PubMed Web of Science ®Google Scholar
• Reed, S. I.. 1996. G1/S regulatory mechanisms from yeast to man. Prog. Cell Cycle Res. 2:15–27
   PubMedGoogle Scholar
• Rubin, H., Yao, A., and Chow, M.. 1995. Neoplastic development: paradoxical relation between impaired cell growth at low population density and excessive growth at high density. Proc. Natl. Acad. Sci. USA 92:7734–7738
   PubMedGoogle Scholar
• Saha, P., Eichbaum, Q., Silberman, E. D., Mayer, B. J., and Dutta, A.. 1997. p21CIP1 and Cdc25A: competition between an inhibitor and an activator of cyclin-dependent kinases. Mol. Cell. Biol. 17:4338–4345
   PubMedGoogle Scholar
• Sambrook, J., Fritsch, E. F., and Maniatis, T.. 1989. Molecular cloning: a laboratory Manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y
   Google Scholar
• Sherr, C. J.. 1993. Mammalian G1 cyclins. Cell 73:1059–1065
   PubMed Web of Science ®Google Scholar
• Sherr, C. J., and Roberts, J. M.. 1995. Inhibitors of mammalian G1 cyclin-dependent kinases. Genes Dev. 9:1149–1163
   PubMed Web of Science ®Google Scholar
• Shockett, P., Difilippantonio, M., Hellman, N., and Schatz, D. G.. 1995. A modified tetracycline-regulated system provides autoregulatory, inducible gene expression in cultured cells and transgenic mice. Proc. Natl. Acad. Sci. USA 92:6522–6526
   PubMed Web of Science ®Google Scholar
• Sugrue, M. M., Shin, D. Y., Lee, S. W., and Aaronson, S. A.. 1997. Wild-type p53 triggers a rapid senescence program in human tumor cells lacking functional p53. Proc. Natl. Acad. Sci. USA 94:9648–9653
   PubMed Web of Science ®Google Scholar
• Taules, M., Rius, E., Talaya, D., Lopez-Girona, A., Bachs, O., and Agell, N.. 1998. Calmodulin is essential for cyclin-dependent kinase 4 (Cdk4) activity and nuclear accumulation of cyclin D1-cdk4 during G1. J. Biol. Chem. 273:33279–33286
   PubMedGoogle Scholar
• Wieser, R. J., Faust, D., Dietrich, C., and Oesch, F.. 1999. p16INK4 mediates contact-inhibition of growth. Oncogene 18:277–281
   PubMedGoogle Scholar
• Wieser, R. J., Schutz, S., Tschank, G., Thomas, H., Dienes, H. P., and Oesch, F.. 1990. Isolation and characterization of a 60–70-kD plasma membrane glycoprotein involved in the contact-dependent inhibition of growth. J. Cell Biol. 111:2681–2692
   PubMedGoogle Scholar
• Yamada, K. M.. 1997. Integrin signaling. Matrix Biol. 16:137–141
   PubMed Web of Science ®Google Scholar
• Yanagisawa, K., Kosaka, A., Iwahana, H., Nakanishi, M., and Tominaga, S.. 1999. Opposite regulation of the expression of cyclin-dependent kinase inhibitors during contact inhibition. J. Biochem. (Tokyo) 125:36–40
   PubMedGoogle Scholar
• Zhu, L., van-den-Heuvel, S., Helin, K., Fattaey, A., Ewen, M., Livingston, D., Dyson, N., and Harlow, E.. 1993. Inhibition of cell proliferation by p107, a relative of the retinoblastoma protein. Genes Dev. 7:1111–1125
   PubMed Web of Science ®Google Scholar