Phosphoprotein expression profiles in rat kidney injury: Source for potential mechanistic biomarkers

Gryshkova, Vitalina; Cotter, Mabel; McGhan, Portia; Obajdin, Jana; Fleurance, Renaud; Costa, André Nogueira da

doi:10.1111/jcmm.14103

Cited by 1 publication

(1 citation statement)

References 11 publications

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“…The role of this phospho-site is matter of debate. It was observed by analyzing phosphorylation sites in mitosis [78,79], in embryonic stem cell differentiation [95], in human cancer cells [80], in 2-Deoxyglucose-stimulated cells [206], as well as in rat models of drug-induced kidney injury caused by cisplatin and puromycin [207]. The Thr394 residue is located within the sequence 389-LNQPGTPTRI-397 in the COOH-terminal tail which could represent a recognition motif for the kinase upstream MEK2 or a cellular translocation signal [187].…”

Section: Dual Specificity Mitogen-activated Protein Kinase Kinase 2 (Map2k2; Uniprot: P36507)mentioning

confidence: 99%

Phosphorylation Sites in Protein Kinases and Phosphatases Regulated by Formyl Peptide Receptor 2 Signaling

Annunziata

Parisi

Esposito

et al. 2020

IJMS

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FPR1, FPR2, and FPR3 are members of Formyl Peptides Receptors (FPRs) family belonging to the GPCR superfamily. FPR2 is a low affinity receptor for formyl peptides and it is considered the most promiscuous member of this family. Intracellular signaling cascades triggered by FPRs include the activation of different protein kinases and phosphatase, as well as tyrosine kinase receptors transactivation. Protein kinases and phosphatases act coordinately and any impairment of their activation or regulation represents one of the most common causes of several human diseases. Several phospho-sites has been identified in protein kinases and phosphatases, whose role may be to expand the repertoire of molecular mechanisms of regulation or may be necessary for fine-tuning of switch properties. We previously performed a phospho-proteomic analysis in FPR2-stimulated cells that revealed, among other things, not yet identified phospho-sites on six protein kinases and one protein phosphatase. Herein, we discuss on the selective phosphorylation of Serine/Threonine-protein kinase N2, Serine/Threonine-protein kinase PRP4 homolog, Serine/Threonine-protein kinase MARK2, Serine/Threonine-protein kinase PAK4, Serine/Threonine-protein kinase 10, Dual specificity mitogen-activated protein kinase kinase 2, and Protein phosphatase 1 regulatory subunit 14A, triggered by FPR2 stimulation. We also describe the putative FPR2-dependent signaling cascades upstream to these specific phospho-sites.

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Section: Dual Specificity Mitogen-activated Protein Kinase Kinase 2 (Map2k2; Uniprot: P36507)mentioning

confidence: 99%

Phosphorylation Sites in Protein Kinases and Phosphatases Regulated by Formyl Peptide Receptor 2 Signaling

Annunziata

Parisi

Esposito

et al. 2020

IJMS

View full text Add to dashboard Cite

show abstract

Phosphoprotein expression profiles in rat kidney injury: Source for potential mechanistic biomarkers

Cited by 1 publication

References 11 publications

Phosphorylation Sites in Protein Kinases and Phosphatases Regulated by Formyl Peptide Receptor 2 Signaling

Phosphorylation Sites in Protein Kinases and Phosphatases Regulated by Formyl Peptide Receptor 2 Signaling

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