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Nucleocytoplasmic Communication

Histone Deacetylase 4 Possesses Intrinsic Nuclear Import and Export Signals

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Pages 5992-6005 | Received 27 Nov 2000, Accepted 30 May 2001, Published online: 27 Mar 2023

REFERENCES

  • Altschul, S. F., T. L. Madden, A. A. Schaffer, J. Zhang, Z. Zhang, W. Miller, and D. J. Lipman. 1997. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 25:3389–3402.
  • Bogerd, H. P., R. A. Fridell, R. E. Benson, J. Hua, and B. R. Cullen. 1996. Protein sequence requirements for function of the human T-cell leukemia virus type 1 Rex nuclear export signal delineated by a novel in vivo randomization-selection assay. Mol. Cell. Biol. 16:4207–4214.
  • Brown, C. E., T. Lechner, L. Howe, and J. L. Workman. 2000. The many HATs of transcription coactivators. Trends Biochem. Sci. 25:15–19.
  • Buggy, J. J., M. L. Sideris, P. Mak, D. D. Lorimer, B. McIntosh, and J. M. Clark. 2000. Cloning and characterization of a novel human histone deacetylase, HDAC8. Biochem. J. 350:199–205.
  • Champagne, N., N. R. Bertos, N. Pelletier, A. H. Wang, M. Vezmar, Y. Yang, H. H. Heng, and X. J. Yang. 1999. Identification of a human histone acetyltransferase related to monocytic leukemia zinc finger protein. J. Biol. Chem. 274:28528–28536.
  • Champagne, N., N. Pelletier, and X. J. Yang. 2001. The monocytic leukemia zinc finger protein MOZ is a histone acetyltransferase. Oncogene 20:404–409.
  • Cheng, Y. S., C. E. Patterson, and P. Staeheli. 1991. Interferon-induced guanylate-binding proteins lack an N(T)KXD consensus motif and bind GMP in addition to GDP and GTP. Mol. Cell. Biol. 11:4717–4725.
  • Cress, W. D., and E. Seto. 2000. Histone deacetylases, transcriptional control, and cancer. J. Cell. Physiol. 184:1–16.
  • Dangond, F., D. A. Hafler, J. K. Tong, J. Randall, R. Kojima, N. Utku, and S. R. Gullans. 1998. Differential display cloning of a novel human histone deacetylase (HDAC3) cDNA from PHA-activated immune cells. Biochem. Biophys. Res. Commun. 242:648–652.
  • Dingwall, C., and R. A. Laskey. 1991. Nuclear targeting sequences-a consensus?. Trends Biochem. Sci. 16:478–481.
  • Dressel, U., P. J. Bailey, S. C. Wang, M. Downes, R. M. Evans, and G. E. Muscat. 2001. A dynamic role for HDAC-7 in MEF2 mediated muscle differentiation. J. Biol. Chem. 276:17361–17366.
  • Emiliani, S., W. Fischle, C. Van Lint, Y. Al-Abed, and E. Verdin. 1998. Characterization of a human RPD3 ortholog, HDAC3. Proc. Natl. Acad. Sci. USA 95:2795–2800.
  • Fischle, W., S. Emiliani, M. J. Hendzel, T. Nagase, N. Nomura, W. Voelter, and E. Verdin. 1999. A new family of human histone deacetylases related to Saccharomyces cerevisiae HDA1p. J. Biol. Chem. 274:11713–11720.
  • Fornerod, M., M. Ohno, M. Yoshida, and I. W. Mattaj. 1997. CRM1 is an export receptor for leucine-rich nuclear export signals. Cell 90:1051–1060.
  • Frye, R. A.. 2000. Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins. Biochem. Biophys. Res. Commun. 273:793–798.
  • Fu, H., R. R. Subramanian, and S. C. Masters. 2000. 14-3-3 proteins: structure, function, and regulation. Annu. Rev. Pharmacol. Toxicol. 40:617–647.
  • Gaubatz, S., J. A. Lees, G. J. Lindeman, and D. M. Livingston. 2001. E2F4 is exported from the nucleus in a CRM1-dependent manner. Mol. Cell. Biol. 21:1384–1392.
  • Gorlich, D.. 1998. Transport into and out of the nucleus. EMBO J. 17:2721–2727.
  • Grozinger, C. M., C. A. Hassig, and S. L. Schreiber. 1999. Three proteins define a class of human histone deacetylases related to yeast Hda1p. Proc. Natl. Acad. Sci. USA 96:4868–4873.
  • Grozinger, C. M., and S. L. Schreiber. 2000. Regulation of histone deacetylase 4 and 5 transcriptional activity by 14-3-3-dependent cellular localization. Proc. Natl. Acad. Sci. USA 97:7835–7840.
  • Grunstein, M.. 1997. Histone acetylation in chromatin structure and transcription. Nature 389:349–352.
  • Hu, E., Z. Chen, T. Fredrickson, Y. Zhu, R. Kirkpatrick, G. F. Zhang, K. Johanson, C. M. Sung, R. Liu, and J. Winkler. 2000. Cloning and characterization of a novel human class I histone deacetylase that functions as a transcription repressor. J. Biol. Chem. 275:15254–15264.
  • Huang, E. Y., J. Zhang, E. A. Miska, M. G. Guenther, T. Kouzarides, and M. A. Lazar. 2000. Nuclear receptor corepressors partner with class II histone deacetylases in a Sin3-independent repression pathway. Genes Dev. 14:45–54.
  • Imai, S. I., C. M. Armstrong, M. Kaeberlein, and L. Guarente. 2000. Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature 403:795–800.
  • Kaffman, A., N. M. Rank, E. M. O'Neill, L. S. Huang, and E. K. O'Shea. 1998. The receptor Msn5 exports the phosphorylated transcription factor Pho4 out of the nucleus. Nature 396:482–486.
  • Kalderon, D., B. L. Roberts, W. D. Richardson, and A. E. Smith. 1984. A short amino acid sequence able to specify nuclear localization. Cell 39:499–509.
  • Kao, H. Y., M. Downes, P. Ordentlich, and R. M. Evans. 2000. Isolation of a novel histone deacetylase reveals that class I and class II deacetylases promote SMRT-mediated repression. Genes Dev. 14:55–66.
  • Khochbin, S., A. Verdel, C. Lemercier, and D. Seigneurin-Berny. 2001. Functional significance of histone deacetylase diversity. Curr. Opin. Genet. Dev. 11:162–166.
  • Kouzarides, T.. 2000. Acetylation: a regulatory modification to rival phosphorylation?. EMBO J. 19:1176–1179.
  • Kudo, N., N. Matsumori, H. Taoka, D. Fujiwara, E. P. Schreiner, B. Wolff, M. Yoshida, and S. Horinouchi. 1999. Leptomycin B inactivates CRM1/exportin 1 by covalent modification at a cysteine residue in the central conserved region. Proc. Natl. Acad. Sci. USA 96:9112–9117.
  • Landry, J., A. Sutton, S. T. Tafrov, R. C. Heller, J. Stebbins, L. Pillus, and R. Sternglanz. 2000. The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases. Proc. Natl. Acad. Sci. USA 97:5807–5811.
  • Lemercier, C., A. Verdel, B. Galloo, S. Curtet, M. P. Brocard, and S. Khochbin. 2000. mHDA1/HDAC5 histone deacetylase interacts with and represses MEF2A transcriptional activity. J. Biol. Chem. 275:15594–15599.
  • Lipowsky, G., F. R. Bischoff, P. Schwarzmaier, R. Kraft, S. Kostka, E. Hartmann, U. Kutay, and D. Gorlich. 2000. Exportin 4: a mediator of a novel nuclear export pathway in higher eukaryotes. EMBO J. 19:4362–4371.
  • Lopez-Girona, A., B. Furnari, O. Mondesert, and P. Russell. 1999. Nuclear localization of Cdc25 is regulated by DNA damage and a 14-3-3 protein. Nature 397:172–175.
  • Lu, J., T. A. McKinsey, R. L. Nicol, and E. N. Olson. 2000. Signal-dependent activation of the MEF2 transcription factor by dissociation from histone deacetylases. Proc. Natl. Acad. Sci. USA 97:4070–4075.
  • Lu, J., T. A. McKinsey, C. L. Zhang, and E. N. Olson. 2000. Regulation of skeletal myogenesis by association of the MEF2 transcription factor with class II histone deacetylases. Mol. Cell 6:233–244.
  • Maroun, C. R., D. K. Moscatello, M. A. Naujokas, M. Holgado-Madruga, A. J. Wong, and M. Park. 1999. A conserved inositol phospholipid binding site within the pleckstrin homology domain of the Gab1 docking protein is required for epithelial morphogenesis. J. Biol. Chem. 274:31719–31726.
  • McBlane, F., and J. Boyes. 2000. Stimulation of V(D)J recombination by histone acetylation. Curr. Biol. 10:483–486.
  • McBride, K., C. McDonald, and N. C. Reich. 2000. Nuclear export signal located within the DNA-binding domain of the STAT1 transcription factor. EMBO J. 19:6196–6206.
  • McKinsey, T. A., C. L. Zhang, J. Lu, and E. N. Olson. 2000. Signal-dependent nuclear export of a histone deacetylase regulates muscle differentiation. Nature 408:106–111.
  • McKinsey, T. A., C. L. Zhang, and E. N. Olson. 2000. Activation of the myocyte enhancer factor-2 transcription factor by calcium/calmodulin-dependent protein kinase-stimulated binding of 14-3-3 to histone deacetylase 5. Proc. Natl. Acad. Sci. USA 97:14400–14405.
  • McMurry, M. T., and M. S. Krangel. 2000. A role for histone acetylation in the developmental regulation of VDJ recombination. Science 287:495–498.
  • Miska, E. A., C. Karlsson, E. Langley, S. J. Nielsen, J. Pines, and T. Kouzarides. 1999. HDAC4 deacetylase associates with and represses the MEF2 transcription factor. EMBO J. 18:5099–5107.
  • Muslin, A. J., and H. Xing. 2000. 14-3-3 proteins: regulation of subcellular localization by molecular interference. Cell. Signal. 12:703–709.
  • Nakielny, S., and G. Dreyfuss. 1999. Transport of proteins and RNAs in and out of the nucleus. Cell 99:677–690.
  • Ossareh-Nazari, B., F. Bachelerie, and C. Dargemont. 1997. Evidence for a role of CRM1 in signal-mediated nuclear protein export. Science 278:141–144.
  • Rittinger, K., J. Budman, J. Xu, S. Volinia, L. C. Cantley, S. J. Smerdon, S. J. Gamblin, and M. B. Yaffe. 1999. Structural analysis of 14-3-3 phosphopeptide complexes identifies a dual role for the nuclear export signal of 14-3-3 in ligand binding. Mol. Cell 4:153–166.
  • Rundlett, S. E., A. A. Carmen, R. Kobayashi, S. Bavykin, B. M. Turner, and M. Grunstein. 1996. HDA1 and RPD3 are members of distinct yeast histone deacetylase complexes that regulate silencing and transcription. Proc. Natl. Acad. Sci. USA 93:14503–14508.
  • Smith, J. S., C. B. Brachmann, I. Celic, M. A. Kenna, S. Muhammad, V. J. Starai, J. L. Avalos, J. C. Escalante-Semerena, C. Grubmeyer, C. Wolberger, and J. D. Boeke. 2000. A phylogenetically conserved NAD+-dependent protein deacetylase activity in the Sir2 protein family. Proc. Natl. Acad. Sci. USA 97:6658–6663.
  • Sparrow, D. B., E. A. Miska, E. Langley, S. Reynaud-Deonauth, S. Kotecha, N. Towers, G. Spohr, T. Kouzarides, and T. J. Mohun. 1999. MEF-2 function is modified by a novel co-repressor, MITR. EMBO J. 18:5085–5098.
  • Stade, K., C. S. Ford, C. Guthrie, and K. Weis. 1997. Exportin 1 (Crm1) is an essential nuclear export factor. Cell 90:1041–1050.
  • Sterner, D. E., and S. L. Berger. 2000. Acetylation of histones and transcription-related factors. Microbiol. Mol. Biol. Rev. 64:435–459.
  • Stewart, S., and G. R. Crabtree. 2000. Regulation of the regulators. Nature 408:46–47.
  • Strahl, B. D., and C. D. Allis. 2000. The language of covalent histone modifications. Nature 403:41–45.
  • Struhl, K.. 1998. Histone acetylation and transcriptional regulatory mechanisms. Genes Dev. 12:599–606.
  • Taunton, J., C. A. Hassig, and S. L. Schreiber. 1996. A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p. Science 272:408–411.
  • Van de Wyngaert, I., W. de Vries, A. Kremer, J. Neefs, P. Verhasselt, W. H. Luyten, and S. U. Kass. 2000. Cloning and characterization of human histone deacetylase 8. FEBS Lett. 478:77–83.
  • Verdel, A., S. Curtet, M. P. Brocard, S. Rousseaux, C. Lemercier, M. Yoshida, and S. Khochbin. 2000. Active maintenance of mHDA2/mHDAC6 histone-deacetylase in the cytoplasm. Curr. Biol. 10:747–749.
  • Verdel, A., and S. Khochbin. 1999. Identification of a new family of higher eukaryotic histone deacetylases. Coordinate expression of differentiation-dependent chromatin modifiers. J. Biol. Chem. 274:2440–2445.
  • Wang, A. H., N. R. Bertos, M. Vezmar, N. Pelletier, M. Crosato, H. H. Heng, J. Th'ng, J. Han, and X.-J. Yang. 1999. HDAC4, a human histone deacetylase related to yeast HDA1, is a transcriptional corepressor. Mol. Cell. Biol. 19:7816–7827.
  • Wang, A. H., M. J. Kruhlak, J. Wu, N. R. Bertos, M. Vezmar, B. I. Posner, D. P. Bazett-Jones, and X.-J. Yang. 2000. Regulation of histone deacetylase 4 by binding of 14-3-3 proteins. Mol. Cell. Biol. 20:6904–6912.
  • Wolffe, A. P., and M. A. Matzke. 1999. Epigenetics: regulation through repression. Science 286:481–486.
  • Wynn, T. A., C. M. Nicolet, and D. M. Paulnock. 1991. Identification and characterization of a new gene family induced during macrophage activation. J. Immunol. 147:4384–4392.
  • Yaffe, M. B., and A. E. H. Elia. 2001. Phosphoserine/threonine-binding domains. Curr. Opin. Cell Biol. 13:131–138.
  • Yang, W. M., C. Inouye, Y. Zeng, D. Bearss, and E. Seto. 1996. Transcriptional repression by YY1 is mediated by interaction with a mammalian homolog of the yeast global regulator RPD3. Proc. Natl. Acad. Sci. USA 93:12845–12850.
  • Yang, W. M., Y. L. Yao, J. M. Sun, J. R. Davie, and E. Seto. 1997. Isolation and characterization of cDNAs corresponding to an additional member of the human histone deacetylase gene family. J. Biol. Chem. 272:28001–28007.
  • Youn, H. D., C. M. Grozinger, and J. O. Liu. 2000. Calcium regulates transcriptional repression of myocyte enhancer factor 2 by histone deacetylase 4. J. Biol. Chem. 275:22563–22567.
  • Zhang, C. L., T. A. McKinsey, J. Lu, and E. N. Olson. 2000. Association of COOH-terminal-binding protein (CtBP) and MEF2-interacting transcription repressor (MITR) contributes to transcriptional repression of the MEF2 transcription factor. J. Biol. Chem. 276:35–39.
  • Zhou, X., V. M. Richon, R. A. Rifkind, and P. A. Marks. 2000. Identification of a transcriptional repressor related to the noncatalytic domain of histone deacetylases 4 and 5. Proc. Natl. Acad. Sci. USA 97:1056–1061.
  • Zhou, X., V. M. Richon, A. H. Wang, X. J. Yang, R. A. Rifkind, and P. A. Marks. 2000. Histone deacetylase 4 associates with extracellular signal-regulated kinases 1 and 2, and its cellular localization is regulated by oncogenic Ras. Proc. Natl. Acad. Sci. USA 97:14329–14333.
  • Zhu, J., and F. McKeon. 1999. NF-AT activation requires suppression of Crm1-dependent export by calcineurin. Nature 398:256–260.

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