Casein Kinase 2 interacts with human mitogen- and stress-activated protein kinase MSK1 and phosphorylates it at Multiple sites

Shi, Yan; Han, Guanghui; Wu, Huiling; Ye, Kan; Tian, Zhipeng; Wang, Jiaqi; Shi, Huidong; Ye, Mingliang; Zou, Hanfa; Huo, Keke

doi:10.5483/bmbrep.2009.42.12.840

Cited by 10 publications

(8 citation statements)

References 23 publications

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“…Consistent with this, three residues (Ser750, Ser752, and Ser758) were found to be autophosphorylated by the NTKD upon MSK activation (229). While similar sites in RSK isoforms regulate ERK1/2 docking (302), these sites do not appear to play a similar function in MSK1 (229 (230,330). While the kinase(s) responsible for the phosphorylation of these sites remains to be identified, recent evidence suggest that casein kinase 2 (CK2) regulates MSK1 phosphorylation at multiple C-terminal residues following UV irradiation (162,330).…”

Section: Msksupporting

confidence: 51%

“…While similar sites in RSK isoforms regulate ERK1/2 docking (302), these sites do not appear to play a similar function in MSK1 (229 (230,330). While the kinase(s) responsible for the phosphorylation of these sites remains to be identified, recent evidence suggest that casein kinase 2 (CK2) regulates MSK1 phosphorylation at multiple C-terminal residues following UV irradiation (162,330). Several compounds have been reported to inhibit MSK1/2 in cells (378), but none of them are selective, as they inhibit several kinases related to MSKs.…”

Section: Mskmentioning

confidence: 99%

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Activation and Function of the MAPKs and Their Substrates, the MAPK-Activated Protein Kinases

Cargnello

Roux

2011

Microbiol Mol Biol Rev

2,534

1,619

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SUMMARY The mitogen-activated protein kinases (MAPKs) regulate diverse cellular programs by relaying extracellular signals to intracellular responses. In mammals, there are more than a dozen MAPK enzymes that coordinately regulate cell proliferation, differentiation, motility, and survival. The best known are the conventional MAPKs, which include the extracellular signal-regulated kinases 1 and 2 (ERK1/2), c-Jun amino-terminal kinases 1 to 3 (JNK1 to -3), p38 (α, β, γ, and δ), and ERK5 families. There are additional, atypical MAPK enzymes, including ERK3/4, ERK7/8, and Nemo-like kinase (NLK), which have distinct regulation and functions. Together, the MAPKs regulate a large number of substrates, including members of a family of protein Ser/Thr kinases termed MAPK-activated protein kinases (MAPKAPKs). The MAPKAPKs are related enzymes that respond to extracellular stimulation through direct MAPK-dependent activation loop phosphorylation and kinase activation. There are five MAPKAPK subfamilies: the p90 ribosomal S6 kinase (RSK), the mitogen- and stress-activated kinase (MSK), the MAPK-interacting kinase (MNK), the MAPK-activated protein kinase 2/3 (MK2/3), and MK5 (also known as p38-regulated/activated protein kinase [PRAK]). These enzymes have diverse biological functions, including regulation of nucleosome and gene expression, mRNA stability and translation, and cell proliferation and survival. Here we review the mechanisms of MAPKAPK activation by the different MAPKs and discuss their physiological roles based on established substrates and recent discoveries.

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Section: Msksupporting

confidence: 51%

Section: Mskmentioning

confidence: 99%

Activation and Function of the MAPKs and Their Substrates, the MAPK-Activated Protein Kinases

Cargnello

Roux

2011

Microbiol Mol Biol Rev

2,534

1,619

View full text Add to dashboard Cite

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“…Many of the proteins annotated as known CK2 substrates contain multiple phosphosites that can be recognized by this complex ( Shi et al., 2009 ; Wise et al., 1997 ; Yang et al., 2013 ). In line with this, 20 of the proteins that we predicted as CSNK2A1/CK2a1 and/or CSNK2A2/CK2a2 substrates had six or more confident phosphosites (defined as above) that mapped within sequence motifs that can be recognized by CK2 ( Figure 4 E).…”

Section: Resultsmentioning

confidence: 99%

Kinase Interaction Network Expands Functional and Disease Roles of Human Kinases

et al. 2020

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Summary Protein kinases are essential for signal transduction and control of most cellular processes, including metabolism, membrane transport, motility, and cell cycle. Despite the critical role of kinases in cells and their strong association with diseases, good coverage of their interactions is available for only a fraction of the 535 human kinases. Here, we present a comprehensive mass-spectrometry-based analysis of a human kinase interaction network covering more than 300 kinases. The interaction dataset is a high-quality resource with more than 5,000 previously unreported interactions. We extensively characterized the obtained network and were able to identify previously described, as well as predict new, kinase functional associations, including those of the less well-studied kinases PIM3 and protein O-mannose kinase (POMK). Importantly, the presented interaction map is a valuable resource for assisting biomedical studies. We uncover dozens of kinase-disease associations spanning from genetic disorders to complex diseases, including cancer.

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“…In eukaryotic cells, it has been demonstrated that mitogen activated protein kinase (MAPK) cascades, one of the largest and most important categories of protein kinases, play an important role as universal modules of signal transduction (MAPK group, 2002;Shi et al,2009). MAPKs form terminal components of the prototypical sequential cascades, and are activated by MAPK kinases (MAPKKs) via dual phosphorylating Thr and Tyr residues within TEY or TDY motif located in theactivation loop (T-loop) between kinase subdomain VII and VIII (Kyiakis and Avruch, 1996;Widmann et al, 1999;Davis, 2000;Mishra et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

Comparative genomic analysis of mitogen activated protein kinase gene family in grapevine

et al. 2010

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Mitogen activated protein kinases (MAPKs) are important proteins involved in the signal transduction of extracellular information to intracellular targets, and play a crucial role in the response to biotic and abiotic stresses. Although Arabidopsis MAPKs are used for identification of the putative MAPKs in higher plants, no grapevine MAPK gene nomenclature has yet been appeared in the literature. In this study, we have identified 12 members of grapevine MAPK gene (VvMPK) family via In-silico analysis of current grapevine genome database. The structural comparison of 12 VvMPKs through the analysis of chromosome locations, sequence annotation and paralogous gene pair indicated that VvMPKs have evolved by segmental duplication, rather than by tandem amplification. Although further functional analysis of VvMPKs through in vivo and in vivo experiments will be required, our study provides the basis for future research on the diverse signaling pathways medicated by MAPKs in grapevine.

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Casein Kinase 2 interacts with human mitogen- and stress-activated protein kinase MSK1 and phosphorylates it at Multiple sites

Cited by 10 publications

References 23 publications

Activation and Function of the MAPKs and Their Substrates, the MAPK-Activated Protein Kinases

Activation and Function of the MAPKs and Their Substrates, the MAPK-Activated Protein Kinases

Kinase Interaction Network Expands Functional and Disease Roles of Human Kinases

Comparative genomic analysis of mitogen activated protein kinase gene family in grapevine

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