Molecular recognitions in the MAP kinase cascades

Tanoue, Takuji; Nishida, Eisuke

doi:10.1016/s0898-6568(02)00112-2

Cited by 299 publications

(264 citation statements)

References 85 publications

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“…It has been shown that p38 kinase can interact directly with numerous proteins with high specificity. [26][27][28] This specific interaction is mediated by a binding domain on p38 kinase, known as the CD domain, and a specific interacting motif on the target molecule, known as the D domain. 29 The D domain is found to form a modular structure, which comprises a cluster of positively charged amino-acid residues (LXL motif) surrounded by a hydrophobic region.…”

Section: Discussionmentioning

confidence: 99%

p38 kinase mediates nitric oxide-induced apoptosis of chondrocytes through the inhibition of protein kinase C ζ by blocking autophosphorylation

et al. 2005

Cell Death Differ

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This study investigated the molecular mechanisms underlying inhibition of protein kinase C (PKC) f by p38 kinase during nitric oxide (NO)-induced apoptosis of chondrocytes. Coimmunoprecipitation experiments showed that activation of p38 kinase following addition of an NO donor resulted in a physical association between PKCf and p38 kinase. Direct interaction of p38 kinase with PKCf was confirmed in vitro using p38 kinase and PKCf recombinant proteins. p38 kinase interacts with the regulatory domain of PKCf and its association blocked PKCf autophosphorylation. Micro LC-MS/MS analysis using recombinant proteins indicated that the interaction of p38 kinase with PKCf blocked autophosphorylation of PKCf on Thr-560, which is required for PKCf activation. Collectively, our results demonstrate a novel mechanism of PKCf regulation: following activation by the production of NO, p38 kinase binds directly to the PKCf regulatory domain, preventing PKCf autophosphorylation on Thr-560, thereby inhibiting PKCf activation.

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Section: Discussionmentioning

confidence: 99%

p38 kinase mediates nitric oxide-induced apoptosis of chondrocytes through the inhibition of protein kinase C ζ by blocking autophosphorylation

et al. 2005

Cell Death Differ

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“…MAPKs can recognize and bind certain transcription factor targets by means of a docking (D) domain consisting of a region of basic residues followed by an LXL motif and a hydrophobic region (Sharrocks et al, 2000;Tanoue and Nishida, 2003). Such docking domains, alone or in combination with a conserved FXFP motif downstream of the MAPK phosphorylation site in certain transcription factors, are required for the specificity, efficiency and accuracy of MAPKmediated phosphorylation (Sharrocks et al, 2000;Tanoue and Nishida, 2003). Another MAPK-docking motif, the LXLXXXF motif, exists within the Pointed (PNT) domain of a subset of ETS transcription factors (Seidel and Graves, 2002).…”

Section: Protein Domains Potentially Involved In Stable and Specific mentioning

confidence: 99%

“…Interaction of these docking sites with corresponding motifs in MAPKs could provide a molecular basis for stable and specific MAPK recruitment. A conserved MAPK domain, the common Journal of Cell Science 117 (17) Cano et al, 1995;Yang et al, 1998c;Yang et al, 1998b;Rao and Reddy, 1994 Yang et al, 1998b;Gupta et al, 1996 Jun GST pulldown, CIP Kallunki et al, 1996;Adler et al, 1992;Dai et al, 1995;Cano et al, 1995;Read et al, 1997;Gupta et al, 1996;Kallunki et al, 1994;Sluss et al, 1994;Hibi et al, 1993;Derijard et al, 1994 SAP-2 GST pulldown Ducret et al, 2000 ATF-2 GST pulldown Livingstone et al, 1995;Gupta et al, 1995;Gupta et al, 1996;Raingeaud et al, 1995 JunB GST pulldown Gupta et al, 1996;Kallunki et al, 1996 docking (CD) domain, is often used in the interaction with docking sites in MAPKKs, MKPs (MAPK-phosphatases) and MAPKAPKs (Tanoue and Nishida, 2003). However, whether or not the D domain of particular transcription factors can interact with the CD domain is not known.…”

Section: Protein Domains Potentially Involved In Stable and Specific mentioning

confidence: 99%

“…The main function of MAPK docking sites in transcription factors appears be in promoting the MAPK-mediated phosphorylation of a nearby phosphoacceptor motif (S/TP) within the same transcription factor (Sharrocks et al, 2000;Tanoue and Nishida, 2003). However, docking sites have also been implicated in recruiting MAPKs to phophorylate other proteins in trans.…”

Section: Protein Domains Potentially Involved In Stable and Specific mentioning

confidence: 99%

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MAP kinases as structural adaptors and enzymatic activators in transcription complexes

Edmunds

Mahadevan

2004

Journal of Cell Science

103

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Mitogen-activated protein kinase (MAPK) pathways regulate eukaryotic gene expression in response to extracellular stimuli. MAPKs and their downstream kinases phosphorylate transcription factors, co-regulators and chromatin proteins to initiate transcriptional changes. However, the spatial context in which the MAPKs operate in transcription complexes is poorly understood. Recent findings in budding yeast show that MAPKs can form integral components of transcription complexes and have novel structural functions in addition to phosphorylating local substrates. Hog1p MAPK is stably recruited to target promoters by specific transcription factors in response to osmotic stress, and acts as both a structural adaptor and enzymatic activator driving the assembly and activation of the transcription complex. We review the evidence that suggests a similar bifunctional role for MAPKs in mammalian transcription complexes.

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“…This physical association is often very important for efficient regulatory transactions such as phosphorylation, dephosphorylation or subcellular localization. Often, such interactions are mediated by MAPK-docking sites-short amino acid stretches that are located on MAPKinteracting proteins [17,18] and that bind to one or more of several characterized cognate binding regions on MAPKs [19,20].…”

Section: Introductionmentioning

confidence: 99%

Analysis of mitogen-activated protein kinase activation and interactions with regulators and substrates

Bardwell

Shah

2006

Methods

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Mitogen-activated protein kinase (MAPK) cascades are ubiquitous signal transduction modules in eukaryotes that are of great interest and importance. Here, we summarize some useful methods for the analysis of MAPK signaling, including methods to (1) detect MAPK activation in cells, with an emphasis on using phosphorylation-state-specific antibodies raised against mammalian phosphopeptide sequences to detect the activation of MAPKs in other species; (2) estimate the cellular concentrations of MAPKs and other proteins of interest; (3) detect and quantify the stable physical association of MAPKs with their substrates and regulators, and estimate the relevant dissociation constants; (4) delineate the MAPK-binding regions or domains of MAPK-interacting proteins, with particular emphasis on the identification and verification of MAPK-docking sites. These procedures are broadly applicable to many organisms, including both yeast and mammalian cells.

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Molecular recognitions in the MAP kinase cascades

Cited by 299 publications

References 85 publications

p38 kinase mediates nitric oxide-induced apoptosis of chondrocytes through the inhibition of protein kinase C ζ by blocking autophosphorylation

p38 kinase mediates nitric oxide-induced apoptosis of chondrocytes through the inhibition of protein kinase C ζ by blocking autophosphorylation

MAP kinases as structural adaptors and enzymatic activators in transcription complexes

Analysis of mitogen-activated protein kinase activation and interactions with regulators and substrates

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