A mechanism of AP-1 suppression through interaction of c-Fos with lamin A/C

Genes and Development

Volumn 20, Issue 3, 2006, Pages 307-320

  Ivorra, Carmen ^a,e   Kubicek, Markus ^a,f   González, José M ^a   Sanz González, Silvia M ^a   Álvarez Barrientos, Alberto ^b   O'Connor, José Enrique ^c   Burke, Brian ^d   Andrés, Vicente ^a  

^a INSTITUTO DE BIOMEDICINA DE VALENCIA   (Spain)

^b CENTRO NACIONAL DE INVESTIGACIONES CARDIOVASCULARES CNIC   (Spain)

^c UNIVERSITY OF VALENCIA   (Spain)

^d UNIVERSITY OF FLORIDA   (United States)

^e UNIVERSIDAD CEU CARDENAL HERRERA   (Spain)

^f MEDICAL UNIVERSITY OF VIENNA   (Austria)

Author keywords

AP 1; c Fos; Lamin A C; Leucine zipper; Nuclear envelope; Transcriptional regulation

Indexed keywords

LAMIN A; LAMIN C; PROTEIN C FOS; PROTEIN C JUN; TRANSCRIPTION FACTOR AP 1;

ANIMAL CELL; ARTICLE; CELL CYCLE ARREST; CELL CYCLE REGULATION; CELL GROWTH; CELL LINE; CELL NUCLEUS MEMBRANE; CELL PROLIFERATION; CELLULAR DISTRIBUTION; COMPLEX FORMATION; CONTROLLED STUDY; FEMALE; GROWTH INHIBITION; HUMAN; HUMAN CELL; IN VITRO STUDY; IN VIVO STUDY; INCUBATION TIME; INHIBITION KINETICS; MAMMAL CELL; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DNA BINDING; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; REGULATORY MECHANISM; TRANSCRIPTION REGULATION;

ANIMALS; BASIC-LEUCINE ZIPPER TRANSCRIPTION FACTORS; CELL CYCLE; CELL NUCLEUS; CELLS, CULTURED; CERCOPITHECUS AETHIOPS; COS CELLS; DIMERIZATION; DNA, RECOMBINANT; GENE EXPRESSION REGULATION; HELA CELLS; HUMANS; LAMIN TYPE A; MICROSCOPY, FLUORESCENCE; NUCLEAR LAMINA; PROTEIN BINDING; PROTO-ONCOGENE PROTEINS C-FOS; RECOMBINANT FUSION PROTEINS; TRANSCRIPTION FACTOR AP-1; TRANSCRIPTION, GENETIC; TWO-HYBRID SYSTEM TECHNIQUES;

ANIMALIA; MAMMALIA;

EID: 32044457898     PISSN: 08909369     EISSN: 15495477     Source Type: Journal    
DOI: 10.1101/gad.349506     Document Type: Article

References (44)

1. Angel, P. and Karin, M. 1991. The role of Jun, Fos, and the AP-1 complex in cell-proliferation and transformation. Biochim. Biophys. Acta 1072: 129-157.
2. Angel, P., Baumann, I., Stein, B., Delius, H., Rahmsdorf, H.J., and Herrlich, P. 1987. 12-O-tetradecanoyl-phorbol-13-acetate induction of the human collagenase gene is mediated by an inducible enhancer element located in the 5′-flanking region. Mol. Cell. Biol. 7: 2256-2266.
3. Bergo, M.O., Gavino, B., Ross, J., Schmidt, W.K., Hong, C., Kendall, L.V., Mohr, A., Meta, M., Genant, H., Jiang, Y., et al. 2002. Zmpste24 deficiency in mice causes spontaneous bone fractures, muscle weakness, and a prelamin A processing defect. Proc. Natl. Acad. Sci. 99: 13049-13054.
4. Kip1 in smooth muscle cells from different vascular beds. A potential role in establishing regional phenotypic variance. J. Biol. Chem. 278: 4482-4490.
5. Chinenov, Y. and Kerppola, T.K. 2001. Close encounters of many kinds: Fos-Jun interactions that mediate transcription regulatory specificity. Oncogene 20: 2438-2452.
6. De Sandre-Giovannoli, A., Bernard, R., Cau, P., Navarro, C., Amiel, J., Boccaccio, I., Lyonnet, S., Stewart, C.L., Munnich, A., Le Merrer, M., et al. 2003. Lamin a truncation in Hutchinson-Gilford progeria. Science 300: 2055.
7. Dreuillet, C., Tillit, J., Kress, M., and Ernoult-Lange, M. 2002. In vivo and in vitro interaction between human transcription factor MOK2 and nuclear lamin A/C. Nucleic Acids Res. 30: 4634-4642.
8. Eferl, R. and Wagner, E.F. 2003. AP-1: A double-edged sword in tumorigenesis. Nat. Rev. Cancer 3: 859-868.
9. Eriksson, M., Brown, W.T., Gordon, L.B., Glynn, M.W., Singer, J., Scott, L., Erdos, M.R., Robbins, C.M., Moses, T.Y., Berglund, P., et al. 2003. Recurrent de novo point mutations in lamin A cause Hutchinson-Gilford progeria syndrome. Nature 423: 293-298.
10. Fields, S. and Song, O. 1989. A novel genetic system to detect protein-protein interactions. Nature 340: 245-246.
11. Gorman, C., Padmanabhan, R., and Howard, B.H. 1983. High efficiency DNA-mediated transformation of primate cells. Science 221: 551-553.
12. Grigoriadis, A.E., Wang, Z.Q., Cecchini, M.G., Hofstetter, W., Felix, R., Fleisch, H.A. and Wagner, E.F. 1994. c-Fos: A key regulator of osteoclast-macrophage lineage determination and bone remodeling. Science 266: 443-448.
13. Gruenbaum, Y., Margalit, A., Goldman, R.D., Shumaker, D.K., and Wilson, K.L. 2005. The nuclear lamina comes of age. Nat. Rev. Mol. Cell. Biol. 6: 21-31.
14. Hutchison, C.J. 2002. Lamins: Building blocks or regulators of gene expression? Nat. Rev. Mol. Cell. Biol. 3: 848-858.
15. Johnson, R.S., Spiegelman, B.M., and Papaioannou, V. 1992. Pleiotropic effects of a null mutation in the c-fos proto-oncogene. Cell 71: 577-586.
16. Johnson, B.R., Nitta, R.T., Frock, R.L., Mounkes, L., Barbie, D.A., Stewart, C.L., Harlow, E., and Kennedy, B.K. 2004. A-type lamins regulate retinoblastoma protein function by promoting subnuclear localization and preventing proteasomal degradation. Proc. Natl. Acad. Sci. 101: 9677-9682.
17. Karin, M., Zg, L., and Zandi, E. 1997. AP-1 function and regulation. Curr. Opin. Cell Biol. 9: 240-246.
18. Kennedy, B.K., Barbie, D.A., Classon, M., Dyson, N., and Harlow, E. 2000. Nuclear organization of DNA replication in primary mammalian cells. Genes & Dev. 14: 2855-2868.
19. Kenworthy, A.K. 2001. Imaging protein-protein interactions using fluorescence resonance energy transfer microscopy. Methods 24: 289-296.
20. Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
21. Lupas, A. 1996. Coiled coils: New structures and new functions. Trends Biochem. Sci. 21: 375-382.
22. Ma, J. and Ptashne, M. 1988. Converting a eukaryotic transcriptional inhibitor into an activator. Cell 55: 443-446.
23. Mancini, M.A., Shan, B., Nickerson, J.A., Penman, S., and Lee, W.H. 1994. The retinoblastoma gene product is a cell cycle-dependent, nuclear matrix-associated protein. Proc. Natl. Acad. Sci. 91: 418-422.
24. Mariappan, I. and Parnaik, V.K. 2005. Sequestration of pRb by cyclin D3 causes intranuclear reorganization of lamin A/C during muscle cell differentiation. Mol. Biol. Cell 16: 1948-1960.
25. Markiewicz, E., Dechat, T., Foisner, R., Quinlan, R.A., and Hutchison, C.J. 2002. Lamin A/C binding protein LAP2α is required for nuclear anchorage of retinoblastoma protein. Mol. Biol. Cell 13: 4401-4413.
26. Mical, T.I. and Monteiro, M.J. 1998. The role of sequences unique to nuclear intermediate filaments in the targeting and assembly of human lamin B: Evidence for lack of interaction of lamin B with its putative receptor. J. Cell Sci. 111 (Pt 23): 3471-3485.
27. Moir, R.D., Spann, T.P., Lopez-Soler, R.I., Yoon, M., Goldman, A.E., Khuon, S., and Goldman, R.D. 2000. Review: The dynamics of the nuclear lamins during the cell cycle - Relationship between structure and function. J. Struct. Biol. 129: 324-334.
28. Mounkes, L.C., Kozlov, S., Hernandez, L., Sullivan, T., and Stewart, C.L. 2003. A progeroid syndrome in mice is caused by defects in A-type lamins. Nature 423: 298-301.
29. Newman, J.R. and Keating, A.E. 2003. Comprehensive identification of human bZIP interactions with coiled-coil arrays. Science 300: 2097-2101.
30. Nigg, E.A. 1992. Assembly-disassembly of the nuclear lamina. Curr. Opin. Cell Biol. 4: 105-109.
31. Nikolova, V., Leimena, C., McMahon, A.C., Tan, J.C., Chandar, S., Jogia, D., Kesteven, S.H., Michalicek, J., Otway, R., Verheyen, F., et al. 2004. Defects in nuclear structure and function promote dilated cardiomyopathy in lamin A/C-deficient mice. J. Clin. Invest. 113: 357-369.
32. Ozaki, T., Saijo, M., Murakami, K., Enomoto, H., Taya, Y., and Sakiyama, S. 1994. Complex formation between lamin A and the retinoblastoma gene product: Identification of the domain on lamin A required for its interaction. Oncogene 9: 2649-2653.
33. Pendás, A.M., Zhou, Z., Cadiñanos, J., Freije, J.M., Wang, J., Hultenby, K., Astudillo, A., Wernerson, A., Rodríguez, F., Tryggvason, K., et al. 2002. Defective prelamin A processing and muscular and adipocyte alterations in Zmpste24 metalloproteinase-deficient mice. Nat. Genet. 31: 94-99.
34. Raharjo, W.H., Enarson, P., Sullivan, T., Stewart, C.L., and Burke, B. 2001. Nuclear envelope defects associated with LMNA mutations cause dilated cardiomyopathy and Emery-Dreifuss muscular dystrophy. J. Cell Sci. 114: 4447-4457.
35. Ruther, U., Komitowski, D., Schubert, F.R., and Wagner, E.F. 1989. c-fos expression induces bone tumors in transgenic mice. Oncogene 4: 861-865.
36. Schirmer, E.C., Guan, T., and Gerace, L. 2001. Involvement of the lamin rod domain in heterotypic lamin interactions important for nuclear organization. J. Cell Biol. 153: 479-489.
37. Schreiber, E., Matthias, P., Muller, M.M., and Schaffner, W. 1989. Rapid detection of octamer binding proteins with 'mini-extracts,' prepared from a small number of cells. Nucleic Acids Res. 17: 6419.
38. Sullivan, T., Escalante-Alcalde, D., Bhatt, H., Anver, M., Bhat, N., Nagashima, K., Stewart, C.L., and Burke, B. 1999. Loss of A-type lamin expression compromises nuclear envelope integrity leading to muscular dystrophy. J. Cell Biol. 147: 913-920.
39. Vriz, S., Lemaitre, J.M., Leibovici, M., Thierry, N., and Mechali, M. 1992. Comparative analysis of the intracellular localization of c-Myc, c-Fos, and replicative proteins during cell cycle progression. Mol. Cell Biol. 12: 3548-3555.
40. Wang, Z.Q., Ovitt, C., Grigoriadis, A.E., Mohle-Steinlein, U., Ruther, U., and Wagner, E.F. 1992. Bone and haematopoietic defects in mice lacking c-fos. Nature 360: 741-745.
41. Wang, W., Chevray, P.M., and Nathans, D. 1996. Mammalian Sug1 and c-Fos in the nuclear 26S proteasome. Proc. Natl. Acad. Sci. 93: 8236-8240.
42. Webb, P., Lopez, G.N., Uht, R.M., and Kushner, P.J. 1995. Tamoxifen activation of the estrogen receptor/AP-1 pathway: Potential origin for the cell-specific estrogen-like effects of antiestrogens. Mol. Endocrinol. 9: 443-456.
43. Worman, H.J. and Courvalin, J.C. 2002. The nuclear lamina and inherited disease. Trends Cell Biol. 12: 591-598.
44. Zastrow, M.S., Vlcek, S., and Wilson, K.L. 2004. Proteins that bind A-type lamins: Integrating isolated clues. J. Cell Sci. 117: 979-987.