Distinct Cellular Functions of MK2

REFERENCES

• Ben-Levy, R., S. Hooper, R. Wilson, H. F. Paterson, and C. J. Marshall. 1998. Nuclear export of the stress-activated protein kinase p38 mediated by its substrate MAPKAP kinase-2. Curr. Biol. 8: 1049–1057.
   PubMed Web of Science ®Google Scholar
• Ben-Levy, R., I. A. Leighton, Y. N. Doza, P. Attwood, N. Morrice, C. J. Marshall, and P. Cohen. 1995. Identification of novel phosphorylation sites required for activation of MAPKAP kinase-2. EMBO J. 14: 5920–5930.
   PubMed Web of Science ®Google Scholar
• Benndorf, R., K. Hayess, S. Ryazantsev, M. Wieske, J. Behlke, and G. Lutsch. 1994. Phosphorylation and supramolecular organization of murine small heat shock protein HSP25 abolish its actin polymerization-inhibiting activity. J. Biol. Chem. 269: 20780–20784.
   PubMed Web of Science ®Google Scholar
• Engel, K., A. Kotlyarov, and M. Gaestel. 1998. Leptomycin B-sensitive nuclear export of MAPKAP kinase 2 is regulated by phosphorylation. EMBO J. 17: 3363–3371.
   PubMed Web of Science ®Google Scholar
• Engel, K., H. Schultz, F. Martin, A. Kotlyarov, K. Plath, M. Hahn, U. Heinemann, and M. Gaestel. 1995. Constitutive activation of mitogen-activated protein kinase-activated protein kinase 2 by mutation of phosphorylation sites and an A-helix motif. J. Biol. Chem. 270: 27213–27221.
   PubMedGoogle Scholar
• Hedges, J. C., M. A. Dechert, I. A. Yamboliev, J. L. Martin, E. Hickey, L. A. Weber, and W. T. Gerthoffer. 1999. A role for p38(MAPK)/HSP27 pathway in smooth muscle cell migration. J. Biol. Chem. 274: 24211–24219.
   PubMed Web of Science ®Google Scholar
• Klekotka, P. A., S. A. Santoro, and M. M. Zutter. 2001. Alpha 2 integrin subunit cytoplasmic domain-dependent cellular migration requires p38 MAPK. J. Biol. Chem. 276: 9503–9511.
   PubMed Web of Science ®Google Scholar
• Komatsu, S., N. Murai, G. Totsukawa, M. Abe, K. Akasaka, H. Shimada, and H. Hosoya. 1997. Identification of MAPKAPK homolog (MAPKAPK-4) as a myosin II regulatory light-chain kinase in sea urchin egg extracts. Arch. Biochem. Biophys. 343: 55–62.
   PubMedGoogle Scholar
• Kotlyarov, A., A. Neininger, C. Schubert, R. Eckert, C. Birchmeier, H. D. Volk, and M. Gaestel. 1999. MAPKAP kinase 2 is essential for LPS-induced TNF-alpha biosynthesis. Nat. Cell Biol 1: 94–97.
   PubMed Web of Science ®Google Scholar
• Larochelle, S., and B. Suter. 1995. The Drosophila melanogaster homolog of the mammalian MAPK-activated protein kinase-2 (MAPKAPK-2) lacks a proline-rich N-terminus. Gene 163: 209–214.
   PubMed Web of Science ®Google Scholar
• Lavoie, J. N., E. Hickey, L. A. Weber, and J. Landry. 1993. Modulation of actin microfilament dynamics and fluid phase pinocytosis by phosphorylation of heat shock protein 27. J. Biol. Chem. 268: 24210–24214.
   PubMed Web of Science ®Google Scholar
• Lee, J. C., J. T. Laydon, P. C. McDonnell, T. F. Gallagher, S. Kumar, D. Green, D. McNulty, M. J. Blumenthal, J. R. Heys, S. W. Landvatter, et al. 1994. A protein kinase involved in the regulation of inflammatory cytokine biosynthesis. Nature 372: 739–746.
   PubMed Web of Science ®Google Scholar
• McClay, D. R. 1999. The role of thin filopodia in motility and morphogenesis. Exp. Cell Res. 253: 296–301.
   PubMed Web of Science ®Google Scholar
• McLaughlin, M. M., S. Kumar, P. C. McDonnell, S. Van Horn, J. C. Lee, G. P. Livi, and P. R. Young. 1996. Identification of mitogen-activated protein (MAP) kinase-activated protein kinase-3, a novel substrate of CSBP p38 MAP kinase. J. Biol. Chem. 271: 8488–8492.
   PubMed Web of Science ®Google Scholar
• New, L., Y. Jiang, M. Zhao, K. Liu, W. Zhu, L. J. Flood, Y. Kato, G. C. Parry, and J. Han. 1998. PRAK, a novel protein kinase regulated by the p38 MAP kinase. EMBO J. 17: 3372–3384.
   PubMed Web of Science ®Google Scholar
• Raingeaud, J., S. Gupta, J. S. Rogers, M. Dickens, J. Han, R. J. Ulevitch, and R. J. Davis. 1995. Pro-inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine. J. Biol. Chem. 270: 7420–7426.
   PubMed Web of Science ®Google Scholar
• Schultz, H., K. Engel, and M. Gaestel. 1997. PMA-induced activation of the p42/44ERK- and p38RK-MAP kinase cascades in HL-60 cells is PKC dependent but not essential for differentiation to the macrophage-like phenotype. J. Cell. Physiol. 173: 310–318.
   PubMed Web of Science ®Google Scholar
• Stokoe, D., B. Caudwell, P. T. Cohen, and P. Cohen. 1993. The substrate specificity and structure of mitogen-activated protein (MAP) kinase-activated protein kinase-2. Biochem. J. 296: 843–849.
   PubMedGoogle Scholar
• Stokoe, D., K. Engel, D. G. Campbell, P. Cohen, and M. Gaestel. 1992. Identification of MAPKAP kinase 2 as a major enzyme responsible for the phosphorylation of the small mammalian heat shock proteins. FEBS Lett. 313: 307–313.
   PubMed Web of Science ®Google Scholar
• Tanoue, T., M. Adachi, T. Moriguchi, and E. Nishida. 2000. A conserved docking motif in MAP kinases common to substrates, activators and regulators. Nat. Cell Biol. 2: 110–116.
   PubMed Web of Science ®Google Scholar
• Tanoue, T., R. Maeda, M. Adachi, and E. Nishida. 2001. Identification of a docking groove on ERK and p38 MAP kinases that regulates the specificity of docking interactions. EMBO J. 20: 466–479.
   PubMed Web of Science ®Google Scholar
• Zu, Y. L., F. Wu, A. Gilchrist, Y. Ai, M. E. Labadia, and C. K. Huang. 1994. The primary structure of a human MAP kinase activated protein kinase 2. Biochem. Biophys. Res. Commun. 200: 1118–1124.
   PubMedGoogle Scholar