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Study on Post-translational Modifications of Protein

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biology".

Deadline for manuscript submissions: closed (28 August 2024) | Viewed by 1204

Special Issue Editor


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Guest Editor
Institute of Molecular Medicine I, Medical Faculty, Heinrich Heine University Düsseldorf, 40225 Düsseldorf, Germany
Interests: signal transduction; protein phosphorylation; protein methylation; snRNP biogenesis; apoptosis; autophagy; SMA

Special Issue Information

Dear Colleagues,

The focus of this Special Issue is the study of post-translational protein modifications (PTMs). These modifications, such as phosphorylation, methylation, acetylation, lipidation, glycosylation, sumoylation and ubiquitinylation, which involve catalyzation by specific enzymes after protein translation, can regulate protein function in terms of activity and stability. In particular, the phosphorylation and methylation of proteins are involved in the signal transduction processes of autophagy, apoptosis and RNA metabolism. In this context, the addition of phosphate groups to specific serines or threonines often influences the binding and enzymatic activities of proteins. Proteolytic modification, such as cleavages caused by caspases during apoptosis, can also irreversibly affect protein function. All of these protein modifications play important roles in a wide variety of signaling pathways. In this Special Issue, individual PTMs as well as the interplay between different PTMs will be investigated with respect to activity, stability, localization and structural changes of the target protein.

Dr. Christoph Peter
Guest Editor

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Keywords

  • phosphorylation
  • methylation
  • ubiquitinylation
  • sumoylation
  • proteolytical cleavage

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Published Papers (1 paper)

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Review

20 pages, 6865 KiB  
Review
R-Methylation in Plants: A Key Regulator of Plant Development and Response to the Environment
by Clément Barré-Villeneuve and Jacinthe Azevedo-Favory
Int. J. Mol. Sci. 2024, 25(18), 9937; https://doi.org/10.3390/ijms25189937 - 14 Sep 2024
Viewed by 537
Abstract
Although arginine methylation (R-methylation) is one of the most important post-translational modifications (PTMs) conserved in eukaryotes, it has not been studied to the same extent as phosphorylation and ubiquitylation. Technical constraints, which are in the process of being resolved, may partly explain this [...] Read more.
Although arginine methylation (R-methylation) is one of the most important post-translational modifications (PTMs) conserved in eukaryotes, it has not been studied to the same extent as phosphorylation and ubiquitylation. Technical constraints, which are in the process of being resolved, may partly explain this lack of success. Our knowledge of R-methylation has recently evolved considerably, particularly in metazoans, where misregulation of the enzymes that deposit this PTM is implicated in several diseases and cancers. Indeed, the roles of R-methylation have been highlighted through the analyses of the main actors of this pathway: the PRMT writer enzymes, the TUDOR reader proteins, and potential “eraser” enzymes. In contrast, R-methylation has been much less studied in plants. Even so, it has been shown that R-methylation in plants, as in animals, regulates housekeeping processes such as transcription, RNA silencing, splicing, ribosome biogenesis, and DNA damage. R-methylation has recently been highlighted in the regulation of membrane-free organelles in animals, but this role has not yet been demonstrated in plants. The identified R-met targets modulate key biological processes such as flowering, shoot and root development, and responses to abiotic and biotic stresses. Finally, arginine demethylases activity has mostly been identified in vitro, so further studies are needed to unravel the mechanism of arginine demethylation. Full article
(This article belongs to the Special Issue Study on Post-translational Modifications of Protein)
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