ijms-logo

Journal Browser

Journal Browser

Ubiquitin Receptors and Associated Mechanisms Involved in Targeting Proteins Modified with Diverged Ubiquitin Signals to Distinct Cellular Processes

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

Deadline for manuscript submissions: 20 May 2024 | Viewed by 1248

Special Issue Editor


E-Mail Website
Guest Editor
Institute of Plant and Microbial Biology, Academia Sinica, Taipei, Taiwan
Interests: function and mechanism studies for critical components of the ubiquitin/26S proteasome system

Special Issue Information

Dear Colleagues,

Ubiquitination is a pivotal regulatory mechanism for nearly all major cellular processes. For all eukaryotic organisms, it is essential for the growth and development of and the response to biotic and abiotic stresses. When catalyzing using many conjugation and deconjugation enzymes, the small and evolutionary conserved ubiquitin could be assembled and dynamically modulated on various protein substrates into highly diverged ubiquitin signals: ubiquitin monomer and ubiquitin chains with homogeneous, mixed, or branched linkages of various lengths. Depending on the different ubiquitin signals assembled, the outcomes of modified substrates could be rather distinct such as degradation by 26S proteasome, endocytosis, or the autophagy pathway. Various ubiquitin signals could also provide interfaces for relaying signal transduction pathways or for recruiting epigenetic regulatory and DNA repairing machineries. While the majority of ubiquitination studies focus on conjugation and deconjugation enzyme components and their corresponding physiological functions, little information is available for specific ubiquitin signals assembled on particular substrates in vivo or on corresponding ubiquitin binding factors for deciphering various ubiquitin signals and associated mechanisms en route to various cellular processes. This Special Issue will be focused on ubiquitin signal assembles on specific substrates and ubiquitin binding proteins involved in deciphering various ubiquitin signals for various cellular processes, such as various degradation pathways, signal transduction, epigenetic regulation, and DNA repairing. All related original articles, up-to-date reviews, and methodology papers will all be considered.     

Dr. Hong-yong Fu
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • ubiquitin
  • ubiquitin signals
  • ubiquitin binding
  • ubiquitin receptor
  • 26S proteasome
  • endocytosis
  • autophagy
  • epigenetic regulation
  • DNA repair

Published Papers (1 paper)

Order results
Result details
Select all
Export citation of selected articles as:

Review

18 pages, 1034 KiB  
Review
Lysine Methylation-Dependent Proteolysis by the Malignant Brain Tumor (MBT) Domain Proteins
by Hong Sun and Hui Zhang
Int. J. Mol. Sci. 2024, 25(4), 2248; https://doi.org/10.3390/ijms25042248 - 13 Feb 2024
Viewed by 729
Abstract
Lysine methylation is a major post-translational protein modification that occurs in both histones and non-histone proteins. Emerging studies show that the methylated lysine residues in non-histone proteins provide a proteolytic signal for ubiquitin-dependent proteolysis. The SET7 (SETD7) methyltransferase specifically transfers a methyl group [...] Read more.
Lysine methylation is a major post-translational protein modification that occurs in both histones and non-histone proteins. Emerging studies show that the methylated lysine residues in non-histone proteins provide a proteolytic signal for ubiquitin-dependent proteolysis. The SET7 (SETD7) methyltransferase specifically transfers a methyl group from S-Adenosyl methionine to a specific lysine residue located in a methylation degron motif of a protein substrate to mark the methylated protein for ubiquitin-dependent proteolysis. LSD1 (Kdm1a) serves as a demethylase to dynamically remove the methyl group from the modified protein. The methylated lysine residue is specifically recognized by L3MBTL3, a methyl-lysine reader that contains the malignant brain tumor domain, to target the methylated proteins for proteolysis by the CRL4DCAF5 ubiquitin ligase complex. The methylated lysine residues are also recognized by PHF20L1 to protect the methylated proteins from proteolysis. The lysine methylation-mediated proteolysis regulates embryonic development, maintains pluripotency and self-renewal of embryonic stem cells and other stem cells such as neural stem cells and hematopoietic stem cells, and controls other biological processes. Dysregulation of the lysine methylation-dependent proteolysis is associated with various diseases, including cancers. Characterization of lysine methylation should reveal novel insights into how development and related diseases are regulated. Full article
Show Figures

Figure 1

Back to TopTop