50ebf8bcd8d191f40858aafbc2f7b7aa pmc_35207610.pdf 1d7d631f66dfd45ed6ab43c809e34b6f5d161ff9 pmc_35207610.pdf 8efab7b68f6a55b563e9d11da7b4e6176c6e8993019560e5a6b2cc3ee1680e71 pmc_35207610.pdf Title: (De)Activation (Ir)Reversibly or Degradation: Dynamics of Post-Translational Protein Modifications in Plants Subject: The increasing dynamic functions of post-translational modifications (PTMs) within protein molecules present outstanding challenges for plant biology even at this present day. Protein PTMs are among the first and fastest plant responses to changes in the environment, indicating that the mechanisms and dynamics of PTMs are an essential area of plant biology. Besides being key players in signaling, PTMs play vital roles in gene expression, gene, and protein localization, protein stability and interactions, as well as enzyme kinetics. In this review, we take a broader but concise approach to capture the current state of events in the field of plant PTMs. We discuss protein modifications including citrullination, glycosylation, phosphorylation, oxidation and disulfide bridges, N-terminal, SUMOylation, and ubiquitination. Further, we outline the complexity of studying PTMs in relation to compartmentalization and function. We conclude by challenging the proteomics community to engage in holistic approaches towards identification and characterizing multiple PTMs on the same protein, their interaction, and mechanism of regulation to bring a deeper understanding of protein function and regulation in plants. Keywords: plant post-translational modifications; phosphorylation; N-glycosylation; methionine oxidation; N-terminal acetylation; SUMOylation; ubiquitination Author: Victor Muleya, L. Maria Lois, Hicham Chahtane, Ludivine Thomas, Marco Chiapello and Claudius Marondedze Creator: LaTeX with hyperref Producer: pdfTeX-1.40.21 CreationDate: Tue Feb 22 10:55:33 2022 CET ModDate: Tue Feb 22 10:58:29 2022 CET Tagged: no UserProperties: no Suspects: no Form: none JavaScript: no Pages: 21 Encrypted: no Page size: 595.276 x 841.89 pts (A4) Page rot: 0 File size: 907057 bytes Optimized: no PDF version: 1.7 name type encoding emb sub uni object ID ------------------------------------ ----------------- ---------------- --- --- --- --------- BAMNYG+VnURWPalladioL Type 1 Custom yes yes no 10 0 YIBLPV+URWPalladioL-Bold Type 1 Custom yes yes no 15 0 VZTRWO+URWPalladioL-Roma Type 1 Custom yes yes no 20 0 ZCIMUA+URWPalladioL-Ital Type 1 Custom yes yes no 24 0 MCBCCI+SourceSansRoman-Regular Type 1C Custom yes yes no 32 0 MCBCCM+SourceSansRoman.613wght Type 1C Custom yes yes no 36 0 MCBCCO+SourceSansRoman-Bold Type 1C Custom yes yes no 40 0 PJCGLK+TimesNewRomanPS-BoldItalicMT Type 1C WinAnsi yes yes no 53 0 ICBUDW+URWPalladioL-BoldItal Type 1 Custom yes yes no 81 0 EVOJTU+EURM10 Type 1 Builtin yes yes no 88 0 AOPHAZ+CMSY10 Type 1 Builtin yes yes no 101 0 BCDEEE+PalatinoLinotype-Bold TrueType WinAnsi yes yes no 129 0 BCDFEE+PalatinoLinotype-Roman TrueType WinAnsi yes yes no 133 0 BCDGEE+PalatinoLinotype-Italic TrueType WinAnsi yes yes no 137 0 BCDIEE+PalatinoLinotype-Roman CID TrueType Identity-H yes yes yes 141 0 ArialMT TrueType WinAnsi no no no 148 0 Jhove (Rel. 1.22.1, 2019-04-17) Date: 2022-07-06 02:25:22 CEST RepresentationInformation: pmc_35207610.pdf ReportingModule: PDF-hul, Rel. 1.12.1 (2019-04-17) LastModified: 2022-02-27 18:33:22 CET Size: 907057 Format: PDF Version: 1.7 Status: Well-Formed and valid SignatureMatches: PDF-hul MIMEtype: application/pdf PDFMetadata: Objects: 672 FreeObjects: 1 IncrementalUpdates: 0 DocumentCatalog: PageLayout: SinglePage PageMode: UseNone Outlines: Item: Title: Introduction Destination: edu.harvard.hul.ois.jhove.module.pdf.PdfSimpleObject@4923ab24 Item: Title: Phosphorylation: Regulation of Plant Signalling Processes Destination: edu.harvard.hul.ois.jhove.module.pdf.PdfSimpleObject@44c8afef Item: Title: Function of N-Glycosylation in Plants Destination: edu.harvard.hul.ois.jhove.module.pdf.PdfSimpleObject@7b69c6ba Item: Title: Redox Regulation, Signaling and Functional Significance in Plants Destination: edu.harvard.hul.ois.jhove.module.pdf.PdfSimpleObject@46daef40 Item: Title: Emerging Roles of N-Terminal Acetylation in Plants Destination: edu.harvard.hul.ois.jhove.module.pdf.PdfSimpleObject@12f41634 Item: Title: Protein Ubiquitination in Plants Destination: edu.harvard.hul.ois.jhove.module.pdf.PdfSimpleObject@13c27452 Item: Title: SUMOylation in Plant Development and Stress Responses Destination: edu.harvard.hul.ois.jhove.module.pdf.PdfSimpleObject@262b2c86 Item: Title: Citrullination Discovery and Potential Roles in Plants Destination: edu.harvard.hul.ois.jhove.module.pdf.PdfSimpleObject@371a67ec Item: Title: Concluding Summary Destination: edu.harvard.hul.ois.jhove.module.pdf.PdfSimpleObject@5ed828d Item: Title: References Destination: edu.harvard.hul.ois.jhove.module.pdf.PdfSimpleObject@50d0686 Info: Title: (De)Activation (Ir)Reversibly or Degradation: Dynamics of Post-Translational Protein Modifications in Plants Author: Victor Muleya, L. Maria Lois, Hicham Chahtane, Ludivine Thomas, Marco Chiapello and Claudius Marondedze Subject: The increasing dynamic functions of post-translational modifications (PTMs) within protein molecules present outstanding challenges for plant biology even at this present day. Protein PTMs are among the first and fastest plant responses to changes in the environment, indicating that the mechanisms and dynamics of PTMs are an essential area of plant biology. Besides being key players in signaling, PTMs play vital roles in gene expression, gene, and protein localization, protein stability and interactions, as well as enzyme kinetics. In this review, we take a broader but concise approach to capture the current state of events in the field of plant PTMs. We discuss protein modifications including citrullination, glycosylation, phosphorylation, oxidation and disulfide bridges, N-terminal, SUMOylation, and ubiquitination. Further, we outline the complexity of studying PTMs in relation to compartmentalization and function. We conclude by challenging the proteomics community to engage in holistic approaches towards identification and characterizing multiple PTMs on the same protein, their interaction, and mechanism of regulation to bring a deeper understanding of protein function and regulation in plants. 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