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Protein Networks and Their Signaling

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: 20 June 2025 | Viewed by 1519

Special Issue Editors


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Guest Editor
Department of Biochemistry and Biophysics, University of Rochester Medical Center, Rochester, NY 14642, USA
Interests: cellular and molecular biology; epigenetics; protein biochemistry and structural biology

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Guest Editor
Department of Molecular Medicine and USF Health Byrd Alzheimer's Institute, Morsani College of Medicine, University of South Florida, Tampa, FL 33612, USA
Interests: protein physics; protein folding; protein misfolding; intrinsically disordered proteins; protein function; protein interactions
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Special Issue Information

Dear Colleagues,

The physiological functions in multicellular organisms are regulated by a network of biomolecules and their signaling. One such biomolecule is protein, and it has been found that protein–protein interactions, protein signaling, chromatin (protein–DNA associations), and epigenetic marks are critical to a number of cellular processes to regulate the normal vs. disease state of the organism.

Therefore, it is crucial to explore such networking, their signaling, and regulatory mechanisms in  healthy and disease conditions. The in-depth molecular, biochemical, and  structural understanding of the proteins and their signaling networks  can be utilized to develop better therapeutics to overcome the disease state.

In this Special Issue, we invite researchers to advance or update our  understanding in the field of protein biochemistry, protein–protein interactions, protein–DNA interactions, biomolecules (DNA, RNA), or any other epigenetic factors (PTMs, etc.) which regulate cellular processes by sharing their scientific work. We hope to include work in the area of diseases like osteoarthritis, lung pathology, cancer, autoimmune disease, cardiovascular diseases, diabetes, and neuropathology, but the scope of the Special Issue is not limited to these topics.

Dr. Ashok Kumar
Prof. Dr. Vladimir N. Uversky
Guest Editors

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Keywords

  • protein-protein interaction
  • chromatin/nucleosome
  • signaling
  • protein structure
  • drug design

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Published Papers (1 paper)

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Research

18 pages, 4892 KiB  
Article
Subunits Med12 and Med13 of Mediator Cooperate with Subunits SAYP and Bap170 of SWI/SNF in Active Transcription in Drosophila
by Yulii V. Shidlovskii, Yulia A. Ulianova, Alexander V. Shaposhnikov, Valeria V. Kolesnik, Anna E. Pravednikova, Nikita G. Stepanov, Darya Chetverina, Giuseppe Saccone, Lyubov A. Lebedeva, Victor K. Chmykhalo and Ennio Giordano
Int. J. Mol. Sci. 2024, 25(23), 12781; https://doi.org/10.3390/ijms252312781 - 28 Nov 2024
Viewed by 997
Abstract
SAYP and Bap170, subunits of the SWI/SNF remodeling complex, have the ability to support enhancer-dependent transcription when artificially recruited to the promoter on a transgene. We found that the phenomenon critically depends on two subunits of the Mediator kinase module, Med12 and Med13 [...] Read more.
SAYP and Bap170, subunits of the SWI/SNF remodeling complex, have the ability to support enhancer-dependent transcription when artificially recruited to the promoter on a transgene. We found that the phenomenon critically depends on two subunits of the Mediator kinase module, Med12 and Med13 but does not require the two other subunits of the module (Cdk8 and CycC) or other subunits of the core part of the complex. A cooperation of the above proteins in active transcription was also observed at endogenous loci, but the contribution of the subunits to the activity of a particular gene differed in different loci. The factors SAYP/Bap170 and Med12/Med13 did not form sufficiently stable interactions in the extract, and their cooperation was apparently local at regulatory elements, the presence of SAYP and Bap170 in a locus being necessary for stable recruitment of Med12 and Med13 to the locus. In addition to the above factors, the Nelf-A protein was found to participate in the process. The cooperation of the factors, independent of enzymatic activities of the complexes they are part of, appears to be a novel mechanism that maintains promoter activity and may be used in many loci of the genome. Extended intrinsically disordered regions of the factors were assumed to sustain the mechanism. Full article
(This article belongs to the Special Issue Protein Networks and Their Signaling)
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