Cross-talk between protein kinase A and the MAPK-activated protein kinases RSK1 and MK5

References

• Skalhegg BS, Tasken K. Specificity in the cAMP/PKA signaling pathway. Differential expression, regulation, and subcellular localization of subunits of PKA. Front Biosci 2000, 5, D678–D693.
   PubMed Web of Science ®Google Scholar
• Taskén K, Aandahl EM. Localized effects of cAMP mediated by distinct routes of protein kinase A. Physiol Rev 2004, 84, 137–167.
   PubMed Web of Science ®Google Scholar
• Johnson GL, Lapadat R. Mitogen-activated protein kinase pathways mediated by ERK, JNK, and p38 protein kinases. Science 2002, 298, 1911–1912.
   PubMed Web of Science ®Google Scholar
• Roux PP, Blenis J. ERK and p38 MAPK-activated protein kinases: a family of protein kinases with diverse biological functions. Microbiol Mol Biol Rev 2004, 68, 320–344.
   PubMed Web of Science ®Google Scholar
• Imajo M, Tsuchiya Y, Nishida E. Regulatory mechanisms and functions of MAP kinase signaling pathways. IUBMB Life 2006, 58, 312–317.
   PubMed Web of Science ®Google Scholar
• Zhang Y, Dong C. Regulatory mechanisms of mitogen-activated kinase signaling. Cell Mol Life Sci 2007, 64, 2771–2789.
   PubMed Web of Science ®Google Scholar
• Krishna M, Narang H. The complexity of mitogen-activated protein kinases (MAPKs) made simple. Cell Mol Life Sci 2008, 65, 3525–3544.
   PubMed Web of Science ®Google Scholar
• Arthur JS. MSK activation and physiological roles. Front Biosci 2008, 13, 5866–5879.
   PubMed Web of Science ®Google Scholar
• Buxade M, Parra-Palau JL, Proud CG. The Mnks: MAP kinase-interacting kinases (MAP kinase signal-integrating kinases). Front Biosci 2008, 13, 5359–5373.
   PubMed Web of Science ®Google Scholar
• Carriere A, Ray H, Blenis J, Roux PP. The RSK factors of activating the Ras/MAPK signaling cascade. Front Biosci 2008, 13, 4258–4275.
   PubMed Web of Science ®Google Scholar
• Ronkina N, Kotlyarov A, Gaestel M. MK2 and MK3–a pair of isoenzymes? Front Biosci 2008, 13, 5511–5521.
   PubMed Web of Science ®Google Scholar
• Vermeulen L, Berghe WV, Beck IM, De Bosscher K, Haegeman G. The versatile role of MSKs in transcriptional regulation. Trends Biochem Sci 2009, 34, 311–318.
   PubMed Web of Science ®Google Scholar
• Raman M, Chen W, Cobb MH. Differential regulation and properties of MAPKs. Oncogene 2007, 26, 3100–3112.
   PubMed Web of Science ®Google Scholar
• Anjum R, Blenis J. The RSK family of kinases: emerging roles in cellular signalling. Nat Rev Mol Cell Biol 2008, 9, 747–758.
   PubMed Web of Science ®Google Scholar
• Gaestel M, Kotlyarov A, Kracht M. Targeting innate immunity protein kinase signalling in inflammation. Nat Rev Drug Discov 2009, 8, 480–499.
   PubMed Web of Science ®Google Scholar
• Gaestel M. MAPKAP kinases - MKs - two’s company, three’s a crowd. Nat Rev Mol Cell Biol 2006, 7, 120–130.
   PubMed Web of Science ®Google Scholar
• Ronkina N, Kotlyarov A, Dittrich-Breiholz O, Kracht M, Hitti E, Milarski K, Askew R, Marusic S, Lin LL, Gaestel M, Telliez JB. The mitogen-activated protein kinase (MAPK)-activated protein kinases MK2 and MK3 cooperate in stimulation of tumor necrosis factor biosynthesis and stabilization of p38 MAPK. Mol Cell Biol 2007, 27, 170–181.
   PubMed Web of Science ®Google Scholar
• Kotlyarov A, Neininger A, Schubert C, Eckert R, Birchmeier C, Volk HD, Gaestel M. MAPKAP kinase 2 is essential for LPS-induced TNF-alpha biosynthesis. Nat Cell Biol 1999, 1, 94–97.
   PubMed Web of Science ®Google Scholar
• Luig C, Köther K, Eva Dudek S, Gaestel M, Hiscott J, Wixler V, Ludwig S. MAP kinase-activated protein kinases 2 and 3 are required for influenza A virus propagation and act via inhibition of PKR. FASEB J 2010. [Epub ahead of print]
   Google Scholar
• Ni H, Wang XS, Diener K, Yao Z. MAPKAPK-5, a novel mitogen-activated protein kinase (MAPK)-activated protein kinase, is a substrate of the extracellular-regulated kinase (ERK) and p38 kinase. Biochem Biophys Res Commun 1998, 243, 492–496.
   PubMed Web of Science ®Google Scholar
• New L, Jiang Y, Zhao M, Liu K, Zhu W, Flood LJ, Kato Y, Parry GC, Han J. PRAK, a novel protein kinase regulated by the p38 MAP kinase. EMBO J 1998, 17, 3372–3384.
   PubMed Web of Science ®Google Scholar
• Gerits N, Shiryaev A, Kostenko S, Klenow H, Shiryaeva O, Johannessen M, Moens U. The transcriptional regulation and cell-specific expression of the MAPK-activated protein kinase MK5. Cell Mol Biol Lett 2009, 14, 548–574.
   Google Scholar
• Perander M, Keyse SM, Seternes OM. Does MK5 reconcile classical and atypical MAP kinases? Front Biosci 2008, 13, 4617–4624.
   PubMedGoogle Scholar
• Dingar D, Benoit MJ, Mamarbachi AM, Villeneuve LR, Gillis MA, Grandy S, Gaestel M, Fiset C, Allen BG. Characterization of the expression and regulation of MK5 in the murine ventricular myocardium. Cell Signal 2010, 22, 1063–1075.
   Google Scholar
• Shiryaev A, Moens U. Mitogen-activated protein kinase p38 and MK2, MK3 and MK5: ménage à trois or ménage à quatre? Cell Signal 2010, 22, 1185–1192.
   PubMedGoogle Scholar
• Chaturvedi D, Poppleton HM, Stringfield T, Barbier A, Patel TB. Subcellular localization and biological actions of activated RSK1 are determined by its interactions with subunits of cyclic AMP-dependent protein kinase. Mol Cell Biol 2006, 26, 4586–4600.
   PubMed Web of Science ®Google Scholar
• Chaturvedi D, Cohen MS, Taunton J, Patel TB. The PKARIalpha subunit of protein kinase A modulates the activation of p90RSK1 and its function. J Biol Chem 2009, 284, 23670–23681.
   PubMed Web of Science ®Google Scholar
• Gerits N, Kostenko S, Shiryaev A, Johannessen M, Moens U. Relations between the mitogen-activated protein kinase and the cAMP-dependent protein kinase pathways: comradeship and hostility. Cell Signal 2008, 20, 1592–1607.
   Google Scholar
• Kirschner LS, Carney JA, Pack SD, Taymans SE, Giatzakis C, Cho YS, Cho-Chung YS, Stratakis CA. Mutations of the gene encoding the protein kinase A type I-alpha regulatory subunit in patients with the Carney complex. Nat Genet 2000, 26, 89–92.
   PubMed Web of Science ®Google Scholar
• Seternes OM, Johansen B, Hegge B, Johannessen M, Keyse SM, Moens U. Both binding and activation of p38 mitogen-activated protein kinase (MAPK) play essential roles in regulation of the nucleocytoplasmic distribution of MAPK-activated protein kinase 5 by cellular stress. Mol Cell Biol 2002, 22, 6931–6945.
   PubMedGoogle Scholar
• Seternes OM, Mikalsen T, Johansen B, Michaelsen E, Armstrong CG, Morrice NA, Turgeon B, Meloche S, Moens U, Keyse SM. Activation of MK5/PRAK by the atypical MAP kinase ERK3 defines a novel signal transduction pathway. EMBO J 2004, 23, 4780–4791.
   PubMed Web of Science ®Google Scholar
• Schumacher S, Laass K, Kant S, Shi Y, Visel A, Gruber AD, Kotlyarov A, Gaestel M. Scaffolding by ERK3 regulates MK5 in development. EMBO J 2004, 23, 4770–4779.
   PubMed Web of Science ®Google Scholar
• Kant S, Schumacher S, Singh MK, Kispert A, Kotlyarov A, Gaestel M. Characterization of the atypical MAPK ERK4 and its activation of the MAPK-activated protein kinase MK5. J Biol Chem 2006, 281, 35511–35519.
   PubMed Web of Science ®Google Scholar
• Gerits N, Mikalsen T, Kostenko S, Shiryaev A, Johannessen M, Moens U. Modulation of F-actin rearrangement by the cyclic AMP/cAMP-dependent protein kinase (PKA) pathway is mediated by MAPK-activated protein kinase 5 and requires PKA-induced nuclear export of MK5. J Biol Chem 2007, 282, 37232–37243.
   Google Scholar
• Déléris P, Rousseau J, Coulombe P, Rodier G, Tanguay PL, Meloche S. Activation loop phosphorylation of the atypical MAP kinases ERK3 and ERK4 is required for binding, activation and cytoplasmic relocalization of MK5. J Cell Physiol 2008, 217, 778–788.
   PubMed Web of Science ®Google Scholar
• http://www.proteinatlas.org
   Google Scholar
• New L, Jiang Y, Han J. Regulation of PRAK subcellular location by p38 MAP kinases. Mol Biol Cell 2003, 14, 2603–2616.
   PubMedGoogle Scholar
• Tanoue T, Maeda R, Adachi M, Nishida E. Identification of a docking groove on ERK and p38 MAP kinases that regulates the specificity of docking interactions. EMBO J 2001, 20, 466–479.
   PubMed Web of Science ®Google Scholar
• Li Q, Zhang N, Zhang D, Wang Y, Lin T, Wang Y, Zhou H, Ye Z, Zhang F, Lin SC, Han J. Determinants that control the distinct subcellular localization of p38alpha-PRAK and p38beta-PRAK complexes. J Biol Chem 2008, 283, 11014–11023.
   Google Scholar
• Julien C, Coulombe P, Meloche S. Nuclear export of ERK3 by a CRM1-dependent mechanism regulates its inhibitory action on cell-cycle progression. J Biol Chem 2003, 278, 42615–42624.
   PubMedGoogle Scholar
• Aberg E, Perander M, Johansen B, Julien C, Meloche S, Keyse SM, Seternes OM. Regulation of MAPK-activated protein kinase 5 activity and subcellular localization by the atypical MAPK ERK4/MAPK4. J Biol Chem 2006, 281, 35499–35510.
   PubMed Web of Science ®Google Scholar
• Kostenko S, Shiryaev A, Gerits N, Dumitriu G, Klenow H, Johannessen M, Moens U. Serine residue 115 of MAPK-activated protein kinase MK5 is crucial for its PKA-regulated nuclear export and biological functions. Cell Mol Life Sci 2010 (In Press).
   Google Scholar
• Doehn U, Gammeltoft S, Shen SH, Jensen CJ. p90 ribosomal S6 kinase 2 is associated with and dephosphorylated by protein phosphatase 2Cdelta. Biochem J 2004, 382, 425–431.
   Google Scholar
• Sun M, Wei Y, Yao L, Xie J, Chen X, Wang H, Jiang J, Gu J. Identification of extracellular signal-regulated kinase 3 as a new interaction partner of cyclin D3. Biochem Biophys Res Commun 2006, 340, 209–214.
   PubMedGoogle Scholar
• Hansen CA, Bartek J, Jensen S. A functional link between the human cell-cycle-regulatory phosphatase Cdc14A and the atypical mitogen-activated kinase Erk3. Cell Cycle 2008, 7, 325–334.
   PubMed Web of Science ®Google Scholar
• Kostenko S, Johannessen M, Moens U. PKA-induced F-actin rearrangement requires phosphorylation of Hsp27 by the MAPKAP kinase MK5. Cell Signal 2009, 21, 712–718.
   Google Scholar
• Kostenko S, Moens U. Heat shock protein 27 phosphorylation: kinases, phosphatases, functions and pathology. Cell Mol Life Sci 2009, 66, 3289–3307.
   PubMed Web of Science ®Google Scholar
• Shiryaev A, Dumitriu G, Moens U. Journal of Molecular Signaling; in press.
   Google Scholar
• Sun P, Yoshizuka N, New L, Moser BA, Li Y, Liao R, Xie C, Chen J, Deng Q, Yamout M, Dong MQ, Frangou CG, Yates JR 3rd, Wright PE, Han J. PRAK is essential for ras-induced senescence and tumor suppression. Cell 2007, 128, 295–308.
   PubMed Web of Science ®Google Scholar
• el-Deiry WS, Tokino T, Velculescu VE, Levy DB, Parsons R, Trent JM, Lin D, Mercer WE, Kinzler KW, Vogelstein B. WAF1, a potential mediator of p53 tumor suppression. Cell 1993, 75, 817–825.
   PubMed Web of Science ®Google Scholar
• Stork PJ, Schmitt JM. Cross-talk between cAMP and MAP kinase signaling in the regulation of cell proliferation. Trends Cell Biol 2002, 12, 258–266.
   PubMed Web of Science ®Google Scholar
• Chen G, Hitomi M, Han J, Stacey DW. The p38 pathway provides negative feedback for Ras proliferative signaling. J Biol Chem 2000, 275, 38973–38980.
   PubMedGoogle Scholar
• Underwood KW, Parris KD, Federico E, Mosyak L, Czerwinski RM, Shane T, Taylor M, Svenson K, Liu Y, Hsiao CL, Wolfrom S, Maguire M, Malakian K, Telliez JB, Lin LL, Kriz RW, Seehra J, Somers WS, Stahl ML. Catalytically active MAP KAP kinase 2 structures in complex with staurosporine and ADP reveal differences with the autoinhibited enzyme. Structure 2003, 11, 627–636.
   PubMedGoogle Scholar
• Cheng R, Felicetti B, Palan S, Toogood-Johnson I, Scheich C, Barker J, Whittaker M, Hesterkamp T. High-resolution crystal structure of human Mapkap kinase 3 in complex with a high affinity ligand. Protein Sci 2010, 19, 168–173.
   Google Scholar
• Howe AK. Regulation of actin-based cell migration by cAMP/PKA. Biochim Biophys Acta 2004, 1692, 159–174.
   PubMed Web of Science ®Google Scholar
• Seino S, Shibasaki T. PKA-dependent and PKA-independent pathways for cAMP-regulated exocytosis. Physiol Rev 2005, 85, 1303–1342.
   PubMed Web of Science ®Google Scholar
• Abel T, Nguyen PV. Regulation of hippocampus-dependent memory by cyclic AMP-dependent protein kinase. Prog Brain Res 2008, 169, 97–115.
   Google Scholar
• Johannessen M, Moens U. Transcription of genes in response to activated cAMP/protein kinase A signalling pathway: there is more to it than CREB. In: Caplin D, ed. Trends in Cellular Signalling. New York, Nova Science Publishers, 2005, 41–78.
   Google Scholar
• Bjørgo E, Taskén K. Novel mechanism of signaling by CD28. Immunol Lett 2010, 129, 1–6.
   PubMedGoogle Scholar
• Movsesian MA, Bristow MR. Alterations in cAMP-mediated signaling and their role in the pathophysiology of dilated cardiomyopathy. Curr Top Dev Biol 2005, 68, 25–48.
   PubMed Web of Science ®Google Scholar
• Farquhar MJ, Harris HJ, Diskar M, Jones S, Mee CJ, Nielsen SU, Brimacombe CL, Molina S, Toms GL, Maurel P, Howl J, Herberg FW, van Ijzendoorn SC, Balfe P, McKeating JA. Protein kinase A-dependent step(s) in hepatitis C virus entry and infectivity. J Virol 2008, 82, 8797–8811.
   PubMed Web of Science ®Google Scholar
• Naviglio S, Caraglia M, Abbruzzese A, Chiosi E, Di Gesto D, Marra M, Romano M, Sorrentino A, Sorvillo L, Spina A, Illiano G. Protein kinase A as a biological target in cancer therapy. Expert Opin Ther Targets 2009, 13, 83–92.
   PubMed Web of Science ®Google Scholar
• Lavogina D, Enkvist E, Uri A. Bisubstrate inhibitors of protein kinases: from principle to practical applications. ChemMedChem 2010, 5, 23–34.
   PubMed Web of Science ®Google Scholar
• Nguyen TL. Targeting RSK: an overview of small molecule inhibitors. Anticancer Agents Med Chem 2008, 8, 710–716.
   PubMed Web of Science ®Google Scholar
• Kostenko S, Khan MT, Sylte I, Moens U. The diterpenoid alkaloid noroxoaconitine is a Mapkap kinase 5 (MK5/PRAK) inhibitor. Cell Mol Life Sci 2010. [Epub ahead of print]
   Google Scholar
• Carlson CR, Lygren B, Berge T, Hoshi N, Wong W, Taskén K, Scott JD. Delineation of type I protein kinase A-selective signaling events using an RI anchoring disruptor. J Biol Chem 2006, 281, 21535–21545.
   PubMed Web of Science ®Google Scholar
• McConnachie G, Langeberg LK, Scott JD. AKAP signaling complexes: getting to the heart of the matter. Trends Mol Med 2006, 12, 317–323.
   PubMed Web of Science ®Google Scholar
• Beene DL, Scott JD. A-kinase anchoring proteins take shape. Curr Opin Cell Biol 2007, 19, 192–198.
   PubMed Web of Science ®Google Scholar