دورية أكاديمية
أعرض في EDS

Isoform-specific optical activation of kinase function reveals p38-ERK signaling crosstalk.

التفاصيل البيبلوغرافية
العنوان: Isoform-specific optical activation of kinase function reveals p38-ERK signaling crosstalk.
المؤلفون: Zhou W; Department of Chemistry, University of Pittsburgh Pittsburgh PA 15260 USA deiters@pitt.edu., Ryan A; Department of Chemistry, University of Pittsburgh Pittsburgh PA 15260 USA deiters@pitt.edu., Janosko CP; Department of Chemistry, University of Pittsburgh Pittsburgh PA 15260 USA deiters@pitt.edu., Shoger KE; Department of Immunology, University of Pittsburgh School of Medicine Pittsburgh PA 15260 USA.; Center for Systems Immunology, University of Pittsburgh Pittsburgh PA 15261 USA., Haugh JM; Department of Chemical and Biomolecular Engineering, North Carolina State University Raleigh NC 27606 USA., Gottschalk RA; Department of Immunology, University of Pittsburgh School of Medicine Pittsburgh PA 15260 USA.; Center for Systems Immunology, University of Pittsburgh Pittsburgh PA 15261 USA., Deiters A; Department of Chemistry, University of Pittsburgh Pittsburgh PA 15260 USA deiters@pitt.edu.; Center for Systems Immunology, University of Pittsburgh Pittsburgh PA 15261 USA.
المصدر: RSC chemical biology [RSC Chem Biol] 2023 Aug 25; Vol. 4 (10), pp. 765-773. Date of Electronic Publication: 2023 Aug 25 (Print Publication: 2023).
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Royal Society of Chemistry Country of Publication: England NLM ID: 101768727 Publication Model: eCollection Cited Medium: Internet ISSN: 2633-0679 (Electronic) Linking ISSN: 26330679 NLM ISO Abbreviation: RSC Chem Biol Subsets: PubMed not MEDLINE
أسماء مطبوعة: Original Publication: Cambridge : Royal Society of Chemistry, [2020]-
مستخلص: Evolution has diversified the mammalian proteome by the generation of protein isoforms that originate from identical genes, e.g. , through alternative gene splicing or post-translational modifications, or very similar genes found in gene families. Protein isoforms can have either overlapping or unique functions and traditional chemical, biochemical, and genetic techniques are often limited in their ability to differentiate between isoforms due to their high similarity. This is particularly true in the context of highly dynamic cell signaling cascades, which often require acute spatiotemporal perturbation to assess mechanistic details. To that end, we describe a method for the selective perturbation of the individual protein isoforms of the mitogen-activated protein kinase (MAPK) p38. The genetic installation of a photocaging group at a conserved active site lysine enables the precise light-controlled initiation of kinase signaling, followed by investigation of downstream events. Through optical control, we have identified a novel point of crosstalk between two major signaling cascades: the p38/MAPK pathway and the extracellular signal-regulated kinase (ERK)/MAPK pathway. Specifically, using the photoactivated p38 isoforms, we have found the p38γ and p38δ variants to be positive regulators of the ERK signaling cascade, while confirming the p38α and p38β variants as negative regulators.
Competing Interests: There are no conflicts to declare.
(This journal is © The Royal Society of Chemistry.)
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معلومات مُعتمدة: R01 AI175067 United States AI NIAID NIH HHS; R35 GM146896 United States GM NIGMS NIH HHS
تواريخ الأحداث: Date Created: 20231006 Latest Revision: 20240210
رمز التحديث: 20240210
مُعرف محوري في PubMed: PMC10549237
DOI: 10.1039/d2cb00157h
PMID: 37799579
قاعدة البيانات: MEDLINE
الوصف
تدمد:2633-0679
DOI:10.1039/d2cb00157h