Subunit 3 of the COP9 Signalosome Is Poised to Facilitate Communication between the Extracellular Matrix and the Nucleus through the Muscle-Specific β1D Integrin

References

• Bao ZZ, Lakonishok M, Kaufman S, Horwitz AF. Alpha 7 beta 1 integrin is a component of the myotendinous junction on skeletal muscle. J Cell Sci. 1993; 106(Pt 2)579–589
   PubMedGoogle Scholar
• Baudoin C., Van der Flier A., Borradori L., Sonnenberg A. Genomic organization of the mouse beta 1 gene: Conservation of the beta 1D but not of the beta 1B and beta 1C integrin splice variants. Cell Adhes Commun. 1996; 4: 1–11
   PubMed Web of Science ®Google Scholar
• Bech-Otschir D., Seeger M., Dubiel W. The COP9 signalosome: At the interface between signal transduction and ubiquitin-dependent proteolysis. J Cell Sci. 2002; 115: 467–473
   PubMed Web of Science ®Google Scholar
• Belkin A.M., Retta S.F. beta1D integrin inhibits cell cycle progression in normal myoblasts and fibroblasts. J Biol Chem. 1998; 273: 15234–15240
   PubMed Web of Science ®Google Scholar
• Belkin A.M., Retta S.F., Pletjushkina O.Y., Balzac F., Silengo L., Fassler R., Koteliansky V.E., Burridge K., Tarone G. Muscle beta1D integrin reinforces the cytoskeleton-matrix link: Modulation of integrin adhesive function by alternative splicing. J Cell Biol. 1997; 139: 1583–1595
   PubMed Web of Science ®Google Scholar
• Bianchi E., Denti S., Granata A., Bossi G., Geginat J., Villa A., Rogge L., Pardi R. Integrin LFA-1 interacts with the transcriptional co-activator JAB1 to modulate AP-1 activity. Nature. 2000; 404: 617–621
   PubMed Web of Science ®Google Scholar
• Cachaco A.S., Chuva de Sousa Lopes S.M., Kuikman I., Bajanca F., Abe K., Baudoin C., Sonnenberg A., Mummery C.L., Thorsteinsdottir S. Knock-in of integrin beta 1D affects primary but not secondary myogenesis in mice. Development. 2003; 130: 1659–1671
   PubMed Web of Science ®Google Scholar
• Chamovitz D.A., Glickman M. The COP9 signalosome. Curr Biol. 2002; 12: R232
   PubMed Web of Science ®Google Scholar
• Chamovitz D.A., Segal D. JAB1/CSN5 and the COP9 signalosome. A complex situation. EMBO Rep. 2001; 2: 96–101
   PubMedGoogle Scholar
• Claret F.X., Hibi M., Dhut S., Toda T., Karin M. A new group of conserved coactivators that increase the specificity of AP-1 transcription factors. Nature. 1996; 383: 453–457
   PubMed Web of Science ®Google Scholar
• Denti S., Sirri A., Cheli A., Rogge L., Innamorati G., Putignano S., Fabbri M., Pardi R., Bianchi E. RanBPM is a phosphoprotein that associates with the plasma membrane and interacts with the integrin LFA-1. J Biol Chem. 2004; 279: 13027–13034
   PubMed Web of Science ®Google Scholar
• Elsea S.H., Mykytyn K., Ferrell K., Coulter K.L., Das P., Dubiel W., Patel P.I., Metherall J.E. Hemizygosity for the COP9 signalosome subunit gene, SGN3, in the Smith-Magenis syndrome. Am J Med Genet. 1999; 87: 342–348
   PubMed Web of Science ®Google Scholar
• Fields S., Song O. A novel genetic system to detect protein-protein interactions. Nature. 1989; 340: 245–246
   PubMed Web of Science ®Google Scholar
• Gimond C., Baudoin C., Sonnenberg A. Defects in adhesion and migration, but not in proliferation and differentiation, of embryonic stem cells upon replacement of integrin subunit beta1A by beta1D. Differentiation. 2000; 66: 93–105
   PubMed Web of Science ®Google Scholar
• Gullberg D., Velling T., Lohikangas L., Tiger C.F. Integrins during muscle development and in muscular dystrophies. Front Biosci. 1998; 3: D1039–D1050
   PubMedGoogle Scholar
• Hong X., Xu L., Li X., Zhai Z., Shu H. CSN3 interacts with IKKgamma and inhibits TNF- but not IL-1-induced NF-kappaB activation. FEBS Lett. 2001; 499: 133–136
   PubMed Web of Science ®Google Scholar
• Hynes R.O. Integrins: Versatility, modulation, and signaling in cell adhesion. Cell. 1992; 69: 11–25
   PubMed Web of Science ®Google Scholar
• Ingber D. Integrins as mechanochemical transducers. Curr Opin Cell Biol. 1991; 3: 841–848
   PubMed Web of Science ®Google Scholar
• Kapelari B., Bech-Otschir D., Hegerl R., Schade R., Dumdey R., Dubiel W. Electron microscopy and subunit-subunit interaction studies reveal a first architecture of COP9 signalosome. J Mol Biol. 2000; 300: 1169–1178
   PubMed Web of Science ®Google Scholar
• Kuppuswamy D., Kerr C., Narishige T., Kasi V.S., Menick D.R., Cooper G.T. Association of tyrosine-phosphorylated c-Src with the cytoskeleton of hypertrophying myocardium. J Biol Chem. 1997; 272: 4500–4508
   PubMed Web of Science ®Google Scholar
• Lee J.W., Choi H.S., Gyuris J., Brent R., Moore D.D. Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor. Mol Endocrinol. 1995; 9: 243–254
   PubMed Web of Science ®Google Scholar
• Levinson H., Sil A.K., Conwell J.E., Hopper J.E., Ehrlich H.P. Alpha V integrin prolongs collagenase production through Jun activation binding protein 1. Ann Plast Surg. 2004; 53: 155–161
   PubMed Web of Science ®Google Scholar
• Liang F., Atakilit A., Gardner D.G. Integrin dependence of brain natriuretic peptide gene promoter activation by mechanical strain. J Biol Chem. 2000; 275: 20355–20360
   PubMed Web of Science ®Google Scholar
• Liliental J., Chang D.D. Rack1, a receptor for activated protein kinase C, interacts with integrin beta subunit. J Biol Chem. 1998; 273: 2379–2383
   PubMed Web of Science ®Google Scholar
• MacKenna D.A., Dolfi F., Vuori K., Ruoslahti E. Extracellular signal-regulated kinase and c-Jun NH2-terminal kinase activation by mechanical stretch is integrin-dependent and matrix-specific in rat cardiac fibroblasts. J Clin Invest. 1998; 101: 301–310
   PubMed Web of Science ®Google Scholar
• Mahalingam S., Ayyavoo V., Patel M., Kieber-Emmons T., Kao G.D., Muschel R.J., Weiner D.B. HIV-1 Vpr interacts with a human 34-kDa mov34 homologue, a cellular factor linked to the G2/M phase transition of the mammalian cell cycle. Proc Natl Acad Sci U S A. 1998; 95: 3419–3424
   PubMed Web of Science ®Google Scholar
• Naumann M., Bech-Otschir D., Huang X., Ferrell K., Dubiel W. COP9 signalosome-directed c-Jun activation/stabilization is independent of JNK. J Biol Chem. 1999; 274: 35297–35300
   PubMed Web of Science ®Google Scholar
• Otey C.A., Pavalko F.M., Burridge K. An interaction between alpha-actinin and the beta 1 integrin subunit in vitro. J Cell Biol. 1990; 111: 721–729
   PubMed Web of Science ®Google Scholar
• Ross R.S., Pham C., Shai S.Y., Goldhaber J.I., Fenczik C., Glembotski C.C., Ginsberg M.H., Loftus J.C. Beta1 integrins participate in the hypertrophic response of rat ventricular myocytes. Circ Res. 1998; 82: 1160–1172
   PubMed Web of Science ®Google Scholar
• Sadoshima J., Izumo S. The cellular and molecular response of cardiac myocytes to mechanical stress. Annu Rev Physiol. 1997; 59: 551–571
   PubMedGoogle Scholar
• Seeger M., Kraft R., Ferrell K., Bech-Otschir D., Dumdey R., Schade R., Gordon C., Naumann M., Dubiel W. A novel protein complex involved in signal transduction possessing similarities to 26S proteasome subunits. FASEB J. 1998; 12: 469–478
   PubMed Web of Science ®Google Scholar
• Sonnenberg A. Integrins and their ligands. Curr Top Microbiol Immunol. 1993; 184: 7–35
   PubMedGoogle Scholar
• Spain B.H., Bowdish K.S., Pacal A.R., Staub S.F., Koo D., Chang C.Y., Xie W., Colicelli J. Two human cDNAs, including a homolog of Arabidopsis FUS6 (COP11), suppress G-protein- and mitogen-activated protein kinase-mediated signal transduction in yeast and mammalian cells. Mol Cell Biol. 1996; 16: 6698–6706
   PubMed Web of Science ®Google Scholar
• Sun M., Opavsky M.A., Stewart D.J., Rabinovitch M., Dawood F., Wen W.H., Liu P.P. Temporal response and localization of integrins beta1 and beta3 in the heart after myocardial infarction: Regulation by cytokines. Circulation. 2003; 107: 1046–1052
   PubMed Web of Science ®Google Scholar
• Tomoda K., Kubota Y., Arata Y., Mori S., Maeda M., Tanaka T., Yoshida M., Yoneda-Kato N., Kato J.Y. The cytoplasmic shuttling and subsequent degradation of p27Kip1 mediated by Jab1/CSN5 and the COP9 signalosome complex. J Biol Chem. 2002; 277: 2302–2310
   PubMed Web of Science ®Google Scholar
• Tsuge T., Matsui M., Wei N. The subunit 1 of the COP9 signalosome suppresses gene expression through its N-terminal domain and incorporates into the complex through the PCI domain. J Mol Biol. 2001; 305: 1–9
   PubMed Web of Science ®Google Scholar
• van der Flier A., Kuikman I., Baudoin C., van der Neut R., Sonnenberg A. A novel beta 1 integrin isoform produced by alternative splicing: Unique expression in cardiac and skeletal muscle. FEBS Lett. 1995; 369: 340–344
   PubMed Web of Science ®Google Scholar
• Wang N., Butler J.P., Ingber D.E. Mechanotransduction across the cell surface and through the cytoskeleton. Science. 1993; 260: 1124–1127
   PubMed Web of Science ®Google Scholar
• Wei N., Deng X.W. Making sense of the COP9 signalosome. A regulatory protein complex conserved from Arabidopsis to human. Trends Genet. 1999; 15: 98–103
   PubMed Web of Science ®Google Scholar