Autophosphorylation kinetics of protein kinases

Wang, Zhixin; Wu, Jiawei

doi:10.1042/bj20020557

Cited by 35 publications

(42 citation statements)

References 41 publications

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“…Many biochemical analyses demonstrate that almost all PKs catalyze intra/inter-molecular autophosphorylation reactions (27). Actually, in our previous report, many Arabidopsis PKs showed the Ser/Thr autophosphorylation activity (17).…”

Section: Identification Of Tyr Autophosphorylation Protein Kinases Usmentioning

confidence: 99%

Members of the Plant CRK Superfamily Are Capable of Trans- and Autophosphorylation of Tyrosine Residues

Nemoto

Takemori

Seki

et al. 2015

Journal of Biological Chemistry

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Background: Protein kinases that catalyze Tyr phosphorylation in plants in vivo are largely unknown. Results: CDPK/CPK-related protein kinases (CRKs) that auto/trans-phosphorylate Tyr residues and six substrates of these were identified. CRK knock-out mutants show reduced Tyr phosphorylation of ␤-tubulin proteins. Conclusion: CRKs can phosphorylate Tyr residues of ␤-tubulin and certain transcription factors. Significance: CRKs might be responsible for much of the protein Tyr phosphorylation in vivo.

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Section: Identification Of Tyr Autophosphorylation Protein Kinases Usmentioning

confidence: 99%

Members of the Plant CRK Superfamily Are Capable of Trans- and Autophosphorylation of Tyrosine Residues

Nemoto

Takemori

Seki

et al. 2015

Journal of Biological Chemistry

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“…Reverse rate constants were calculated based on established dissociation constants. Apparent K m and k cat values were calculated by globally fitting data at all complex concentrations simultaneously, as described elsewhere (24). At complex concentrations above 4 M, data were excluded from further analysis as significant inhibition of autophosphorylation was observed.…”

mentioning

confidence: 99%

Molecular Framework for the Activation of RNA-dependent Protein Kinase

McKenna

Lindhout

Kim

et al. 2007

Journal of Biological Chemistry

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The RNA-dependent protein kinase (PKR) plays an integral role in the antiviral response to cellular infection. PKR contains three distinct domains consisting of two conserved N-terminal double-stranded RNA (dsRNA)-binding domains, a C-terminal Ser-Thr kinase domain, and a central 80-residue linker. Despite rich structural and biochemical data, a detailed mechanistic explanation of PKR activation remains unclear. Here we provide a framework for understanding dsRNA-dependent activation of PKR using nuclear magnetic resonance spectroscopy, dynamic light scattering, gel filtration, and autophosphorylation kinetics. In the latent state, PKR exists as an extended monomer, with an increase in self-affinity upon dsRNA association. Subsequent phosphorylation leads to efficient release of dsRNA followed by a greater increase in self-affinity. Activated PKR displays extensive conformational perturbations within the kinase domain. We propose an updated model for PKR activation in which the communication between RNA binding, central linker, and kinase domains is critical in the propagation of the activation signal and for PKR dimerization.

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“…Autophosphorylation of cellular kinases can occur intermolecularly or intramolecularly, which will potentially alter the protein conformation, and positively or negatively regulate the catalytic activity of the kinase (Wang and Wu, 2002;Pickin et al, 2008). In addition, phosphorylation of a target kinase can also influence its interaction with other proteins.…”

Section: Viral Proteins Is Phosphorylated By Cellular and Viral Kinasesmentioning

confidence: 99%

The regulatory role of protein phosphorylation in human gammaherpesvirus associated cancers

et al. 2017

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Activation of specific sets of protein kinases by intracellular signal molecules has become more and more apparent in the past decade. Phosphorylation, one of key posttranslational modification events, is activated by kinase or regulatory protein and is vital for controlling many physiological functions of eukaryotic cells such as cell proliferation, differentiation, malignant transformation, and signal transduction mediated by external stimuli. Moreovers, the reversible modification of phosphorylation and dephosphorylation can result in different features of the target substrate molecules including DNA binding, protein-protein interaction, subcellular location and enzymatic activity, and is often hijacked by viral infection. Epstein-Barr virus (EBV) and Kaposi's sarcomaassociated herpesvirus (KSHV), two human oncogenic gamma-herpesviruses, are shown to tightly associate with many malignancies. In this review, we summarize the recent progresses on understanding of molecular properties and regulatory modes of cellular and viral proteins phosphorylation influenced by these two tumor viruses, and highlight the potential therapeutic targets and strategies against their related cancers.

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Autophosphorylation kinetics of protein kinases

Cited by 35 publications

References 41 publications

Members of the Plant CRK Superfamily Are Capable of Trans- and Autophosphorylation of Tyrosine Residues

Members of the Plant CRK Superfamily Are Capable of Trans- and Autophosphorylation of Tyrosine Residues

Molecular Framework for the Activation of RNA-dependent Protein Kinase

The regulatory role of protein phosphorylation in human gammaherpesvirus associated cancers

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