12/6/2023 0 Comments Molecular chaperone definition![]() ![]() Post-translational modification (PTM) is a covalent change in an amino acid in a protein that can modify the properties and functions of the latter, for instance folding, ligand binding, migration to the place of residence, interaction with other molecules, and other specific roles, which in the case of molecular chaperones could be any of the various modes of chaperoning client polypeptides and any of their non-canonical tasks. This is an important topic considering the number of acquired Hsp60 chaperonopathies already cataloged, many of which are serious diseases without efficacious treatment. Future research ought to determine which PTM causes which variations in the Hsp60 molecular properties and functions, and which of them are pathogenic, causing chaperonopathies. Hyperacetylation was associated with mitochondrial failure S-nitrosylation has an impact on mitochondrial stability and endothelial integrity citrullination can be pro-apoptotic oxidation has a role in the response to cellular injury and in cell migration and ubiquitination regulates interaction with the ubiquitin-proteasome system. Nitration was found to affect the stability of the mitochondrial permeability transition pore, to inhibit folding ability, and to perturb insulin secretion. The effect of some of these PTMs on Hsp60 functions have been examined, for instance phosphorylation has been implicated in sperm capacitation, docking of H2B and microtubule-associated proteins, mitochondrial dysfunction, tumor invasiveness, and delay or facilitation of apoptosis. The amino acid sequence of Hsp60 contains many potential phosphorylation sites, and other PTMs are possible such as O-GlcNAcylation, nitration, acetylation, S-nitrosylation, citrullination, oxidation, and ubiquitination. Likely, one factor contributing to this diversity is post-translational modification (PTM). The question is by what mechanism this protein can become multifaceted. Thus, Hsp60 is a multifaceted molecule with a wide range of cellular and tissue locations and functions, which is noteworthy because there is only one hsp60 gene. These non-canonical functions include participation in inflammation, autoimmunity, carcinogenesis, cell replication, and other cellular events in health and disease. In addition to this canonical role, Hsp60 plays many others beyond the mitochondria, for instance in the cytosol, plasma-cell membrane, extracellular space, and body fluids. Hsp60 is a chaperone belonging to the Chaperonins of Group I and typically functions inside mitochondria in which, together with the co-chaperonin Hsp10, maintains protein homeostasis. 4Department of Microbiology and Immunology, School of Medicine, University of Maryland at Baltimore-Institute of Marine and Environmental Technology (IMET), Baltimore, MD, United States.3Department of Medical Chemistry, Medical University of Gdańsk, Gdańsk, Poland.2Euro-Mediterranean Institute of Science and Technology (IEMEST), Palermo, Italy.1Section of Human Anatomy, Department of Biomedicine, Neuroscience and Advanced Diagnostic (BIND), University of Palermo, Palermo, Italy.Celeste Caruso Bavisotto 1,2 Giusi Alberti 1 Alessandra Maria Vitale 1 Letizia Paladino 1 Claudia Campanella 1 Francesca Rappa 1 Magdalena Gorska 3 Everly Conway de Macario 2,4 Francesco Cappello 1,2 Alberto J.
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