دورية أكاديمية
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DUSP3 modulates IRES-dependent translation of mRNAs through dephosphorylation of the HNRNPC protein in cells under genotoxic stimulus.

التفاصيل البيبلوغرافية
العنوان: DUSP3 modulates IRES-dependent translation of mRNAs through dephosphorylation of the HNRNPC protein in cells under genotoxic stimulus.
المؤلفون: Ferruzo PYM; Laboratory of Signaling in Biomolecular Systems, Department of Biochemistry, Institute of Chemistry, University of São Paulo, São Paulo, Brazil., Boell VK; Laboratory of Signaling in Biomolecular Systems, Department of Biochemistry, Institute of Chemistry, University of São Paulo, São Paulo, Brazil., Russo LC; Laboratory of Genome Instability, Department of Biochemistry, Institute of Chemistry, University of São Paulo, São Paulo, Brazil., Oliveira CC; Laboratory of Post-transcriptional Control of Gene Expression, Department of Biochemistry, Institute of Chemistry, University of São Paulo, São Paulo, Brazil., Forti FL; Laboratory of Signaling in Biomolecular Systems, Department of Biochemistry, Institute of Chemistry, University of São Paulo, São Paulo, Brazil.
المصدر: Biology of the cell [Biol Cell] 2024 May; Vol. 116 (5), pp. e2300128. Date of Electronic Publication: 2024 Mar 27.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Wiley-Blackwell Country of Publication: England NLM ID: 8108529 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1768-322X (Electronic) Linking ISSN: 02484900 NLM ISO Abbreviation: Biol Cell Subsets: MEDLINE
أسماء مطبوعة: Publication: 2012- : Chichester : Wiley-Blackwell
Original Publication: Ivry sur Seine France : Publié par la Société française de microscopie électronique avec le concours du Centre national de la recherche scientifique et de l'Institute national de la santé et de la recherche médicale, [1981-
مواضيع طبية MeSH: DNA Damage* , Dual Specificity Phosphatase 3*/metabolism , Dual Specificity Phosphatase 3*/genetics , RNA, Messenger*/genetics , RNA, Messenger*/metabolism , Heterogeneous-Nuclear Ribonucleoprotein Group C*/genetics , Heterogeneous-Nuclear Ribonucleoprotein Group C*/metabolism, Humans ; Heterogeneous-Nuclear Ribonucleoproteins/metabolism ; Heterogeneous-Nuclear Ribonucleoproteins/genetics ; Phosphorylation ; Protein Biosynthesis
مستخلص: Background Information: The dual-specificity phosphatase 3 (DUSP3) regulates cell cycle progression, proliferation, senescence, and DNA repair pathways under genotoxic stress. This phosphatase interacts with HNRNPC protein suggesting an involvement in the regulation of HNRNPC-ribonucleoprotein complex stability. In this work, we investigate the impact of DUSP3 depletion on functions of HNRNPC aiming to suggest new roles for this enzyme.
Results: The DUSP3 knockdown results in the tyrosine hyperphosphorylation state of HNRNPC increasing its RNA binding ability. HNRNPC is present in the cytoplasm where it interacts with IRES trans-acting factors (ITAF) complex, which recruits the 40S ribosome on mRNA during protein synthesis, thus facilitating the translation of mRNAs containing IRES sequence in response to specific stimuli. In accordance with that, we found that DUSP3 is present in the 40S, monosomes and polysomes interacting with HNRNPC, just like other previously identified DUSP3 substrates/interacting partners such as PABP and NCL proteins. By downregulating DUSP3, Tyr-phosphorylated HNRNPC preferentially binds to IRES-containing mRNAs within ITAF complexes preferentially in synchronized or stressed cells, as evidenced by the higher levels of proteins such as c-MYC and XIAP, but not their mRNAs such as measured by qPCR. Under DUSP3 absence, this increased phosphorylated-HNRNPC/RNA interaction reduces HNRNPC-p53 binding in presence of RNAs releasing p53 for specialized cellular responses. Similarly, to HNRNPC, PABP physically interacts with DUSP3 in an RNA-dependent manner.
Conclusions and Significance: Overall, DUSP3 can modulate cellular responses to genotoxic stimuli at the translational level by maintaining the stability of HNRNPC-ITAF complexes and regulating the intensity and specificity of RNA interactions with RRM-domain proteins.
(© 2024 Société Française des Microscopies and Société de Biologie Cellulaire de France. Published by John Wiley & Sons Ltd.)
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معلومات مُعتمدة: Fundação de Amparo à Pesquisa do Estado de São Paulo; Conselho Nacional de Desenvolvimento Científico e Tecnológico; Coordenação de Aperfeiçoamento de Pessoal de Nível Superior
فهرسة مساهمة: Keywords: DUSP3; HNRNPC; genome integrity; mRNA translation; phosphorylation/dephosphorylation; protein synthesis
المشرفين على المادة: EC 3.1.3.48 (Dual Specificity Phosphatase 3)
EC 3.1.3.48 (DUSP3 protein, human)
0 (Heterogeneous-Nuclear Ribonucleoproteins)
0 (RNA, Messenger)
0 (HNRNPC protein, human)
0 (Heterogeneous-Nuclear Ribonucleoprotein Group C)
تواريخ الأحداث: Date Created: 20240327 Date Completed: 20240508 Latest Revision: 20240605
رمز التحديث: 20240606
DOI: 10.1111/boc.202300128
PMID: 38538536
قاعدة البيانات: MEDLINE
الوصف
تدمد:1768-322X
DOI:10.1111/boc.202300128