دورية أكاديمية
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Cysteine S -acetylation is a post-translational modification involved in metabolic regulation.

التفاصيل البيبلوغرافية
العنوان: Cysteine S -acetylation is a post-translational modification involved in metabolic regulation.
المؤلفون: Keenan EK; Duke Molecular Physiology Institute and Sarah W. Stedman Nutrition and Metabolism Center, Duke University Medical Center, Durham NC 27701.; Department of Pharmacology & Cancer Biology, Duke University Medical Center, Durham NC 27710., Bareja A; Duke Molecular Physiology Institute and Sarah W. Stedman Nutrition and Metabolism Center, Duke University Medical Center, Durham NC 27701.; Division of Endocrinology, Metabolism, & Nutrition, Department of Medicine, Duke University, Medical Center, Durham NC 27710., Lam Y; Duke Molecular Physiology Institute and Sarah W. Stedman Nutrition and Metabolism Center, Duke University Medical Center, Durham NC 27701., Grimsrud PA; Duke Molecular Physiology Institute and Sarah W. Stedman Nutrition and Metabolism Center, Duke University Medical Center, Durham NC 27701.; Division of Endocrinology, Metabolism, & Nutrition, Department of Medicine, Duke University, Medical Center, Durham NC 27710., Hirschey MD; Duke Molecular Physiology Institute and Sarah W. Stedman Nutrition and Metabolism Center, Duke University Medical Center, Durham NC 27701.; Department of Pharmacology & Cancer Biology, Duke University Medical Center, Durham NC 27710.; Division of Endocrinology, Metabolism, & Nutrition, Department of Medicine, Duke University, Medical Center, Durham NC 27710.
المصدر: BioRxiv : the preprint server for biology [bioRxiv] 2024 May 21. Date of Electronic Publication: 2024 May 21.
نوع المنشور: Journal Article; Preprint
اللغة: English
بيانات الدورية: Country of Publication: United States NLM ID: 101680187 Publication Model: Electronic Cited Medium: Internet ISSN: 2692-8205 (Electronic) Linking ISSN: 26928205 NLM ISO Abbreviation: bioRxiv Subsets: PubMed not MEDLINE
مستخلص: Cysteine is a reactive amino acid central to the catalytic activities of many enzymes. It is also a common target of post-translational modifications (PTMs), such as palmitoylation. This longchain acyl PTM can modify cysteine residues and induce changes in protein subcellular localization. We hypothesized that cysteine could also be modified by short-chain acyl groups, such as cysteine S -acetylation. To test this, we developed sample preparation and non-targeted mass spectrometry protocols to analyze the mouse liver proteome for cysteine acetylation. Our findings revealed hundreds of sites of cysteine acetylation across multiple tissue types, revealing a previously uncharacterized cysteine acetylome. Cysteine acetylation shows a marked cytoplasmic subcellular localization signature, with tissue-specific acetylome patterns and specific changes upon metabolic stress. This study uncovers a novel aspect of cysteine biochemistry, highlighting short-chain modifications alongside known long-chain acyl PTMs. These findings enrich our understanding of the landscape of acyl modifications and suggest new research directions in enzyme activity regulation and cellular signaling in metabolism.
Competing Interests: COMPETING INTERESTS The authors declare no competing interests.
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معلومات مُعتمدة: R01 AG045351 United States AG NIA NIH HHS; R01 DK115568 United States DK NIDDK NIH HHS; R21 AG080334 United States AG NIA NIH HHS; T32 GM007105 United States GM NIGMS NIH HHS
فهرسة مساهمة: Keywords: Cysteine acetylation; Metabolism; Post-translational modification; Protein acetylation
تواريخ الأحداث: Date Created: 20240603 Latest Revision: 20240717
رمز التحديث: 20240717
مُعرف محوري في PubMed: PMC11142221
DOI: 10.1101/2024.05.21.595030
PMID: 38826225
قاعدة البيانات: MEDLINE
الوصف
تدمد:2692-8205
DOI:10.1101/2024.05.21.595030