دورية أكاديمية
The methylome of motile cilia.
| العنوان: | The methylome of motile cilia. |
|---|---|
| المؤلفون: | King SM; Department of Molecular Biology and Biophysics, University of Connecticut Health Center, Farmington, CT 3305., Sakato-Antoku M; Department of Molecular Biology and Biophysics, University of Connecticut Health Center, Farmington, CT 3305., Patel-King RS; Department of Molecular Biology and Biophysics, University of Connecticut Health Center, Farmington, CT 3305., Balsbaugh JL; Proteomics and Metabolomics Facility, Center for Open Research Resources & Equipment, University of Connecticut, Storrs, CT 06269. |
| المصدر: | Molecular biology of the cell [Mol Biol Cell] 2024 Jul 01; Vol. 35 (7), pp. ar89. Date of Electronic Publication: 2024 May 02. |
| نوع المنشور: | Journal Article |
| اللغة: | English |
| بيانات الدورية: | Publisher: American Society for Cell Biology Country of Publication: United States NLM ID: 9201390 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1939-4586 (Electronic) Linking ISSN: 10591524 NLM ISO Abbreviation: Mol Biol Cell Subsets: MEDLINE |
| أسماء مطبوعة: | Original Publication: Bethesda, MD : American Society for Cell Biology, c1992- |
| مواضيع طبية MeSH: | Cilia*/metabolism , S-Adenosylmethionine*/metabolism , Protein Processing, Post-Translational* , Proteomics*/methods, Methylation ; Animals ; Humans ; Methyltransferases/metabolism ; S-Adenosylhomocysteine/metabolism ; Epigenome |
| مستخلص: | Cilia are highly complex motile, sensory, and secretory organelles that contain perhaps 1000 or more distinct protein components, many of which are subject to various posttranslational modifications such as phosphorylation, N-terminal acetylation, and proteolytic processing. Another common modification is the addition of one or more methyl groups to the side chains of arginine and lysine residues. These tunable additions delocalize the side-chain charge, decrease hydrogen bond capacity, and increase both bulk and hydrophobicity. Methylation is usually mediated by S-adenosylmethionine (SAM)-dependent methyltransferases and reversed by demethylases. Previous studies have identified several ciliary proteins that are subject to methylation including axonemal dynein heavy chains that are modified by a cytosolic methyltransferase. Here, we have performed an extensive proteomic analysis of multiple independently derived cilia samples to assess the potential for SAM metabolism and the extent of methylation in these organelles. We find that cilia contain all the enzymes needed for generation of the SAM methyl donor and recycling of the S-adenosylhomocysteine and tetrahydrofolate byproducts. In addition, we find that at least 155 distinct ciliary proteins are methylated, in some cases at multiple sites. These data provide a comprehensive resource for studying the consequences of methyl marks on ciliary biology. |
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| معلومات مُعتمدة: | R35 GM140631 United States GM NIGMS NIH HHS; S10 OD028445 United States OD NIH HHS |
| المشرفين على المادة: | 7LP2MPO46S (S-Adenosylmethionine) EC 2.1.1.- (Methyltransferases) 979-92-0 (S-Adenosylhomocysteine) |
| تواريخ الأحداث: | Date Created: 20240502 Date Completed: 20240606 Latest Revision: 20240714 |
| رمز التحديث: | 20240714 |
| مُعرف محوري في PubMed: | PMC11244166 |
| DOI: | 10.1091/mbc.E24-03-0130 |
| PMID: | 38696262 |
| قاعدة البيانات: | MEDLINE |
| تدمد: | 1939-4586 |
|---|---|
| DOI: | 10.1091/mbc.E24-03-0130 |