Phosphorylation Sites in Protein Kinases and Phosphatases Regulated by Formyl Peptide Receptor 2 Signaling
| العنوان: | Phosphorylation Sites in Protein Kinases and Phosphatases Regulated by Formyl Peptide Receptor 2 Signaling |
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| المؤلفون: | Melania Parisi, Gabriella Fabbrocini, Maria Carmela Annunziata, Gabriella Esposito, Rosario Ammendola, Fabio Cattaneo |
| المساهمون: | Annunziata, M. C., Parisi, M., Esposito, G., Fabbrocini, G., Ammendola, R., Cattaneo, F. |
| المصدر: | International Journal of Molecular Sciences International Journal of Molecular Sciences, Vol 21, Iss 3818, p 3818 (2020) |
| بيانات النشر: | MDPI AG, 2020. |
| سنة النشر: | 2020 |
| مصطلحات موضوعية: | FPR2, Cell signaling, phospho-sites, Amino Acid Motifs, Phosphatase, Review, MAP2K2, Protein Serine-Threonine Kinases, PPP1R14A, Catalysis, Receptor tyrosine kinase, lcsh:Chemistry, Inorganic Chemistry, MARK2, Phosphoprotein Phosphatases, Animals, Humans, Phospho-site, PRP4, Phosphorylation, Physical and Theoretical Chemistry, Protein kinase A, lcsh:QH301-705.5, Molecular Biology, Spectroscopy, PKN2, G protein-coupled receptor, biology, Chemistry, Kinase, Organic Chemistry, STK10, Protein phosphatase 1, General Medicine, Receptors, Formyl Peptide, Computer Science Applications, Cell biology, lcsh:Biology (General), lcsh:QD1-999, PAK4, biology.protein, Protein Processing, Post-Translational, Signal Transduction |
| الوصف: | 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. |
| تدمد: | 1422-0067 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::688457f394e83ee93eb05f81a29eeedfTest https://doi.org/10.3390/ijms21113818Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....688457f394e83ee93eb05f81a29eeedf |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 14220067 |
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