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Biological Liquid-Liquid Phase Separation, Biomolecular Condensates, and Membraneless Organelles 2.0

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

Deadline for manuscript submissions: 20 May 2024 | Viewed by 1292

Special Issue Editor

Department of Molecular Medicine, USF Health Byrd Alzheimer’s Research Institute, Morsani College of Medicine, University of South Florida, 12901 Bruce B. Downs Blvd, MDC07, Tampa, FL 33612, USA
Interests: intrinsically disordered proteins; protein folding; protein misfolding; partially folded proteins; protein aggregation; protein structure; protein function; protein stability; protein biophysics; protein bioinformatics; conformational diseases; protein–ligand interactions; protein–protein interactions; liquid-liquid phase transitions
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Special Issue Information

Dear Colleagues,

Currently, there is immense interest among the scientific community in intracellular liquid–liquid phase separation (LLPS) and resulting biomolecular condensates (BMCs) and membrane-less organelles (MLOs). Obviously, such BMCs and MLOs, which do not have enclosing membranes, are mysterious subjects, whose components can directly contact, and exchange with, the exterior environment and whose biogenesis and structural integrity rely exclusively on protein–protein and/or protein–nucleic acid interactions. BMCs/MLOs, are large, highly dynamic, macromolecular ensembles visible under the light microscope as spherical micron-sized droplets. They demonstrate liquid-like behavior, being able to drip, formation of spherical structures upon fusion, and wetting. Therefore, MLOs are condensed liquid droplets formed as a result of reversible and highly controlled LLPS. MLOs are different in size, shape, and composition, and have important and diverse biological functions. Typically, MLOs are formed in response to specific cellular activities or stress. Alterations of their biogenesis might have pathological consequences, and many MLOs are associated with the pathogenesis of various diseases. This Special Issue includes research papers and reviews dedicated to the different aspects of LLPS, BMCs, and MLOs.

Prof. Dr. Vladimir N. Uversky
Guest Editor

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Published Papers (1 paper)

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28 pages, 11034 KiB  
Nucleolar- and Nuclear-Stress-Induced Membrane-Less Organelles: A Proteome Analysis through the Prism of Liquid–Liquid Phase Separation
Int. J. Mol. Sci. 2023, 24(13), 11007; https://doi.org/10.3390/ijms241311007 - 02 Jul 2023
Cited by 2 | Viewed by 941
Radical changes in the idea of the organization of intracellular space that occurred in the early 2010s made it possible to consider the formation and functioning of so-called membrane-less organelles (MLOs) based on a single physical principle: the liquid–liquid phase separation (LLPS) of [...] Read more.
Radical changes in the idea of the organization of intracellular space that occurred in the early 2010s made it possible to consider the formation and functioning of so-called membrane-less organelles (MLOs) based on a single physical principle: the liquid–liquid phase separation (LLPS) of biopolymers. Weak non-specific inter- and intramolecular interactions of disordered polymers, primarily intrinsically disordered proteins, and RNA, play a central role in the initiation and regulation of these processes. On the other hand, in some cases, the “maturation” of MLOs can be accompanied by a “liquid–gel” phase transition, where other types of interactions can play a significant role in the reorganization of their structure. In this work, we conducted a bioinformatics analysis of the propensity of the proteomes of two membrane-less organelles, formed in response to stress in the same compartment, for spontaneous phase separation and examined their intrinsic disorder predispositions. These MLOs, amyloid bodies (A-bodies) formed in the response to acidosis and heat shock and nuclear stress bodies (nSBs), are characterized by a partially overlapping composition, but show different functional activities and morphologies. We show that the proteomes of these biocondensates are differently enriched in proteins, and many have high potential for spontaneous LLPS that correlates with the different morphology and function of these organelles. The results of these analyses allowed us to evaluate the role of weak interactions in the formation and functioning of these important organelles. Full article
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