Docking interactions in the mitogen-activated protein kinase cascades.

Regulation of cellular functions and responses utilizes a number of the signal transduction pathways. Each pathway should transduce signals with high efficiency and fidelity to avoid unnecessary crosstalks. The mitogen-activated protein kinase (MAPK) cascades regulate a wide variety of cellular functions, including cell proliferation, differentiation, and stress responses. MAPK is activated by MAPK kinase; phosphorylates various targets, including transcription factors and MAPK-activated protein kinases; and is inactivated by several phosphatases. Recent studies have provided a cue to understand the molecular mechanism underlying the signal transduction through the MAPK cascades. In the MAPK cascades, docking interactions, which are achieved through a site outside the catalytic domain of MAPKs, regulate the efficiency and specificity of the enzymatic reactions. The docking interaction is different from a transient enzyme-substrate interaction through the active center. It has been shown that activators, substrates, and inactivators of MAPKs utilize a common site on MAPKs in the docking interaction. Then, the docking interaction may regulate not only the efficiency and specificity of the cascades, but also the ordered and integrated signaling.

[1]  J. Avruch,et al.  Protein kinase cascades activated by stress and inflammatory cytokines , 1996, BioEssays : news and reviews in molecular, cellular and developmental biology.

[2]  Jonathan A. Cooper,et al.  Protein modification: Docking sites for kinases , 1999, Current Biology.

[3]  Tony Hunter,et al.  MNK1, a new MAP kinase‐activated protein kinase, isolated by a novel expression screening method for identifying protein kinase substrates , 1997, The EMBO journal.

[4]  T. Sturgill,et al.  Recent progress in characterization of protein kinase cascades for phosphorylation of ribosomal protein S6. , 1991, Biochimica et biophysica acta.

[5]  B. Hemmings,et al.  Regulation of protein kinase cascades by protein phosphatase 2A. , 1999, Trends in biochemical sciences.

[6]  M. Muda,et al.  MKP-3, a Novel Cytosolic Protein-tyrosine Phosphatase That Exemplifies a New Class of Mitogen-activated Protein Kinase Phosphatase (*) , 1996, The Journal of Biological Chemistry.

[7]  S. Keyse,et al.  Protein phosphatases and the regulation of mitogen-activated protein kinase signalling. , 2000, Current opinion in cell biology.

[8]  M. Cobb,et al.  Hydrophobic as Well as Charged Residues in Both MEK1 and ERK2 Are Important for Their Proper Docking* , 2001, The Journal of Biological Chemistry.

[9]  E. Nishida,et al.  The MAP kinase cascade is essential for diverse signal transduction pathways. , 1993, Trends in biochemical sciences.

[10]  E. Nishida,et al.  Identification of a docking groove on ERK and p38 MAP kinases that regulates the specificity of docking interactions , 2001, The EMBO journal.

[11]  Jonathan A. Cooper,et al.  Mitogen‐activated protein kinases activate the serine/threonine kinases Mnk1 and Mnk2 , 1997, The EMBO journal.

[12]  E. Nishida,et al.  A Novel MAPK Phosphatase MKP-7 Acts Preferentially on JNK/SAPK and p38α and β MAPKs* , 2001, The Journal of Biological Chemistry.

[13]  E. Nishida,et al.  Molecular Cloning and Characterization of a Novel Dual Specificity Phosphatase, MKP-5* , 1999, The Journal of Biological Chemistry.

[14]  Maria Deak,et al.  The PIF‐binding pocket in PDK1 is essential for activation of S6K and SGK, but not PKB , 2001, The EMBO journal.

[15]  M. Karin,et al.  JNKK1 organizes a MAP kinase module through specific and sequential interactions with upstream and downstream components mediated by its amino-terminal extension. , 1998, Genes & development.

[16]  R. Pulido,et al.  Interaction of Mitogen-activated Protein Kinases with the Kinase Interaction Motif of the Tyrosine Phosphatase PTP-SL Provides Substrate Specificity and Retains ERK2 in the Cytoplasm* , 1999, The Journal of Biological Chemistry.

[17]  P. Caron,et al.  Crystal structure of JNK3: a kinase implicated in neuronal apoptosis. , 1998, Structure.

[18]  T. Hunter,et al.  Signaling—2000 and Beyond , 2000, Cell.

[19]  D. Lawrence,et al.  Multiple Regions of MAP Kinase Phosphatase 3 Are Involved in Its Recognition and Activation by ERK2* , 2001, The Journal of Biological Chemistry.

[20]  C. Der,et al.  The Mitogen-activated Protein Kinase Phosphatases PAC1, MKP-1, and MKP-2 Have Unique Substrate Specificities and Reduced Activity in Vivo toward the ERK2 sevenmaker Mutation (*) , 1996, The Journal of Biological Chemistry.

[21]  K Kornfeld,et al.  Multiple docking sites on substrate proteins form a modular system that mediates recognition by ERK MAP kinase. , 1999, Genes & development.

[22]  Elizabeth J. Goldsmith,et al.  Atomic structure of the MAP kinase ERK2 at 2.3 Å resolution , 1994, Nature.

[23]  E. Hafen,et al.  A gain-of-function mutation in Drosophila MAP kinase activates multiple receptor tyrosine kinase signaling pathways , 1994, Cell.

[24]  K. Irie,et al.  A Novel Kinase Cascade Mediated by Mitogen-activated Protein Kinase Kinase 6 and MKK3* , 1996, The Journal of Biological Chemistry.

[25]  R. Treisman,et al.  Regulation of transcription by MAP kinase cascades. , 1996, Current opinion in cell biology.

[26]  T. Sturgill,et al.  Creation of a Stress-activated p90 Ribosomal S6 Kinase , 2000, The Journal of Biological Chemistry.

[27]  E. Goldsmith,et al.  The structure of mitogen-activated protein kinase p38 at 2.1-A resolution. , 1997, Proceedings of the National Academy of Sciences of the United States of America.

[28]  T. Pawson,et al.  Protein-protein interactions define specificity in signal transduction. , 2000, Genes & development.

[29]  Tony Pawson,et al.  Protein modules and signalling networks , 1995, Nature.

[30]  H. Schaeffer,et al.  Mitogen-Activated Protein Kinases: Specific Messages from Ubiquitous Messengers , 1999, Molecular and Cellular Biology.

[31]  E. Krebs,et al.  The mitogen-activated protein kinase activator. , 1992, Current opinion in cell biology.

[32]  E. Nishida,et al.  A conserved docking motif in MAP kinases common to substrates, activators and regulators , 2000, Nature Cell Biology.

[33]  S. Pelech,et al.  Definition of a consensus sequence for peptide substrate recognition by p44mpk, the meiosis-activated myelin basic protein kinase. , 1991, The Journal of biological chemistry.

[34]  L. Pinna,et al.  How do protein kinases recognize their substrates? , 1996, Biochimica et biophysica acta.

[35]  M. Cobb,et al.  Mitogen-activated protein kinase pathways. , 1997, Current opinion in cell biology.

[36]  M. Muda,et al.  Catalytic activation of the phosphatase MKP-3 by ERK2 mitogen-activated protein kinase. , 1998, Science.

[37]  Masahiko Hibi,et al.  c-Jun Can Recruit JNK to Phosphorylate Dimerization Partners via Specific Docking Interactions , 1996, Cell.

[38]  R. Davis,et al.  Identification of substrate recognition determinants for human ERK1 and ERK2 protein kinases. , 1991, The Journal of biological chemistry.

[39]  Andrew D. Sharrocks,et al.  Targeting of p38 Mitogen-Activated Protein Kinases to MEF2 Transcription Factors , 1999, Molecular and Cellular Biology.

[40]  Y. Nishida,et al.  Genetic analysis of rolled, which encodes a Drosophila mitogen-activated protein kinase. , 1999, Genetics.

[41]  Maria Deak,et al.  Identification of a pocket in the PDK1 kinase domain that interacts with PIF and the C‐terminal residues of PKA , 2000, The EMBO journal.

[42]  A. Sharrocks,et al.  Differential targeting of MAP kinases to the ETS‐domain transcription factor Elk‐1 , 1998, The EMBO journal.

[43]  A. Ullrich,et al.  PTP‐SL and STEP protein tyrosine phosphatases regulate the activation of the extracellular signal‐regulated kinases ERK1 and ERK2 by association through a kinase interaction motif , 1998, The EMBO journal.

[44]  M. Camps,et al.  Dual specificity phosphatases: a gene family for control of MAP kinase function , 2000, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[45]  C. Marshall,et al.  Specificity of receptor tyrosine kinase signaling: Transient versus sustained extracellular signal-regulated kinase activation , 1995, Cell.

[46]  A. Gavin,et al.  A MAP kinase docking site is required for phosphorylation and activation of p90rsk/MAPKAP kinase-1 , 1999, Current Biology.

[47]  P. Kuwabara,et al.  Regulation of dauer larva development in Caenorhabditis elegans by daf-18, a homologue of the tumour suppressor PTEN , 1999, Current Biology.

[48]  T. Sturgill,et al.  Identification of an Extracellular Signal-regulated Kinase (ERK) Docking Site in Ribosomal S6 Kinase, a Sequence Critical for Activation by ERK in Vivo * , 1999, The Journal of Biological Chemistry.

[49]  M. Muda,et al.  The Mitogen-activated Protein Kinase Phosphatase-3 N-terminal Noncatalytic Region Is Responsible for Tight Substrate Binding and Enzymatic Specificity* , 1998, The Journal of Biological Chemistry.

[50]  R. Walther,et al.  Regulation of glucose-6-phosphatase gene expression by protein kinase Balpha and the forkhead transcription factor FKHR. Evidence for insulin response unit-dependent and -independent effects of insulin on promoter activity. , 2000, The Journal of biological chemistry.

[51]  Paul R. Caron,et al.  Crystal Structure of p38 Mitogen-activated Protein Kinase* , 1996, The Journal of Biological Chemistry.

[52]  L. Bardwell,et al.  A conserved motif at the amino termini of MEKs might mediate high-affinity interaction with the cognate MAPKs. , 1996, Trends in biochemical sciences.

[53]  Y. Ip,et al.  Signal transduction by the c-Jun N-terminal kinase (JNK)--from inflammation to development. , 1998, Current opinion in cell biology.

[54]  P. Cohen,et al.  Molecular basis for the substrate specificity of protein kinase B; comparison with MAPKAP kinase‐1 and p70 S6 kinase , 1996, FEBS letters.

[55]  E. Nishida,et al.  Interaction of MAP kinase with MAP kinase kinase: its possible role in the control of nucleocytoplasmic transport of MAP kinase , 1997, The EMBO journal.