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Roles of KCTD Proteins in Biological Processes and Diseases: State of the Art and Future Perspectives

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 (20 October 2023) | Viewed by 1952

Special Issue Editor

Prof. Dr. Terry Hébert

E-Mail Website
Guest Editor
Department of Pharmacology and Therapeutics, McGill University, Montreal, QC H3G 1Y6, Canada
Interests: cellular signalling; G-protein-coupled receptors; stem cells; heart disease; drug discovery

Special Issue Information

Dear Colleagues,

This Special Issue aims to present a comprehensive overview of the latest research on the diverse roles of KCTD proteins in biological processes and diseases. KCTD proteins have recently emerged as important regulators of protein‒protein interactions, and their dysregulation has been linked to several human diseases. The Special Issue will present state-of-the-art research on the influence of KCTD proteins on various biological processes, including neuronal signaling, ion channel modulation, and ubiquitination, among others. It will also cover their implication in several human diseases, including cancer, epilepsy, and brain development disorders. Future perspectives on the potential therapeutic applications of KCTD protein modulation as a means of treating these diseases will be explored.

Additionally, some suggestions for reviews and articles to be included in the Issue include

  1. Structural and functional studies of KCTD proteins;
  2. The role of KCTD proteins in neurological disorders;
  3. KCTD proteins in ubiquitination and their implications in cancer and other diseases;
  4. KCTD proteins in ion channel modulation and their implications in neurological disorders;
  5. KCTD proteins in metabolic disorders;
  6. The regulatory function of KCTD12 in cardiovascular disease;
  7. The genetic and molecular mechanisms of KCTD10 in lung cancer progression;
  8. KCTD7 as a biomarker for Parkinson's disease diagnosis;
  9. KCTD21 in the regulation of adipocyte differentiation and insulin signaling;
  10. The role of KCTD5 in DNA damage repair and cancer therapy.

These suggested topics are not exhaustive, and authors are encouraged to suggest further suitable topics within the scope of the Special Issue. Hopefully, this issue can provide a comprehensive understanding of the significance of KCTD proteins in biological processes and disease pathogenesis, which would be of immense value in the research on the development of new drugs and their potential use in clinical settings.

Prof. Dr. Terry Hébert
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.

Published Papers (2 papers)

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Research

18 pages, 5712 KiB  
Article
A Comprehensive Analysis of the Structural Recognition between KCTD Proteins and Cullin 3
by Nicole Balasco, Luciana Esposito, Giovanni Smaldone, Marco Salvatore and Luigi Vitagliano
Int. J. Mol. Sci. 2024, 25(3), 1881; https://doi.org/10.3390/ijms25031881 - 04 Feb 2024
Viewed by 634
Abstract
KCTD ((K)potassium Channel Tetramerization Domain-containing) proteins constitute an emerging class of proteins involved in fundamental physio-pathological processes. In these proteins, the BTB domain, which represents the defining element of the family, may have the dual role of promoting oligomerization and favoring functionally important [...] Read more.
KCTD ((K)potassium Channel Tetramerization Domain-containing) proteins constitute an emerging class of proteins involved in fundamental physio-pathological processes. In these proteins, the BTB domain, which represents the defining element of the family, may have the dual role of promoting oligomerization and favoring functionally important partnerships with different interactors. Here, by exploiting the potential of recently developed methodologies for protein structure prediction, we report a comprehensive analysis of the interactions of all KCTD proteins with their most common partner Cullin 3 (Cul3). The data here presented demonstrate the impressive ability of this approach to discriminate between KCTDs that interact with Cul3 and those that do not. Indeed, reliable and stable models of the complexes were only obtained for the 15 members of the family that are known to interact with Cul3. The generation of three-dimensional models for all KCTD–Cul3 complexes provides interesting clues on the determinants of the structural basis of this partnership as clear structural differences emerged between KCTDs that bind or do not bind Cul3. Finally, the availability of accurate three-dimensional models for KCTD–Cul3 interactions may be valuable for the ad hoc design and development of compounds targeting specific KCTDs that are involved in several common diseases. Full article
(This article belongs to the Special Issue Roles of KCTD Proteins in Biological Processes and Diseases: State of the Art and Future Perspectives)
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14 pages, 2871 KiB  
Article
KCTD5 Forms Hetero-Oligomeric Complexes with Various Members of the KCTD Protein Family
by Yini Liao, Douglas C. Sloan, Josephine H. Widjaja and Brian S. Muntean
Int. J. Mol. Sci. 2023, 24(18), 14317; https://doi.org/10.3390/ijms241814317 - 20 Sep 2023
Cited by 1 | Viewed by 863
Abstract
Potassium Channel Tetramerization Domain 5 (KCTD5) regulates diverse aspects of physiology, ranging from neuronal signaling to colorectal cancer. A key feature of KCTD5 is its self-assembly into multi-subunit oligomers that seemingly enables participation in an array of protein–protein interactions. KCTD5 has recently been [...] Read more.
Potassium Channel Tetramerization Domain 5 (KCTD5) regulates diverse aspects of physiology, ranging from neuronal signaling to colorectal cancer. A key feature of KCTD5 is its self-assembly into multi-subunit oligomers that seemingly enables participation in an array of protein–protein interactions. KCTD5 has recently been reported to form hetero-oligomeric complexes with two similar KCTDs (KCTD2 and KCTD17). However, it is not known if KCTD5 forms hetero-oligomeric complexes with the remaining KCTD protein family which contains over two dozen members. Here, we demonstrate that KCTD5 interacts with various KCTD proteins when assayed through co-immunoprecipitation in lysed cells. We reinforced this dataset by examining KCTD5 interactions in a live-cell bioluminescence resonance energy transfer (BRET)-based approach. Finally, we developed an IP-luminescence approach to map regions on KCTD5 required for interaction with a selection of KCTD that have established roles in neuronal signaling. We report that different regions on KCTD5 are responsible for uniquely contributing to interactions with other KCTD proteins. While our results help unravel additional interaction partners for KCTD5, they also reveal additional complexities in KCTDs’ biology. Moreover, our findings also suggest that KCTD hetero-oligomeric interactions may occur throughout the KCTD family. Full article
(This article belongs to the Special Issue Roles of KCTD Proteins in Biological Processes and Diseases: State of the Art and Future Perspectives)
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