The HSP90 family: Structure, regulation, function, and implications in health and disease
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MDPI AG
Abstract
The mammalian HSP90 family of proteins is a cluster of highly conserved molecules that are involved in myriad cellular processes. Their distribution in various cellular compartments underlines their essential roles in cellular homeostasis. HSP90 and its co-chaperones orchestrate crucial physiological processes such as cell survival, cell cycle control, hormone signaling, and apoptosis. Conversely, HSP90, and its secreted forms, contribute to the development and progress of serious pathologies, including cancer and neurodegenerative diseases. Therefore, targeting HSP90 is an attractive strategy for the treatment of neoplasms and other diseases. This manuscript will review the general structure, regulation and function of HSP90 family and their potential role in pathophysiology. © 2018 by the authors. Licensee MDPI, Basel, Switzerland.
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Grp94, Hsp90, Molecular chaperones, Pathophysiology, Structure and function, Trap1, Animals, Apoptosis, Cell cycle, Cell survival, Hsp70 heat-shock proteins, Hsp90 heat-shock proteins, Humans, Membrane proteins, Adenosine triphosphatase, Adenosine triphosphate, Calcium, Calmodulin, Chaperone, Divalent cation, Epigallocatechin gallate, Geldanamycin, Guanosine triphosphatase, Heat shock protein 90, Heat shock protein 90 alpha, Heat shock protein 90 alpha a2, Heat shock protein 90 beta, Magnesium, Novobiocin, Protein bcl 2, Radicicol, Somatomedin, Toll like receptor, Transcription factor, Unclassified drug, Glucose-regulated proteins, Heat shock protein 70, Membrane protein, Acetylation, Amino acid sequence, Amino terminal sequence, Biotransformation, Carboxy terminal sequence, Cell cycle regulation, Cell differentiation, Cellular distribution, Chromosome 12, Chromosome 16, Degenerative disease, Dimerization, Gene control, Human, Hydrophobicity, Immune response, Leishmania donovani, Malignant neoplasm, Methylation, Nitrosylation, Oligomerization, Oxidative stress, Parkinson disease, Phosphorylation, Plasmodium falciparum, Protein folding, Protein function, Protein processing, Protein structure, Review, Signal transduction, Sumoylation, Ubiquitination, X ray diffraction, Animal, Chemistry, Genetics, Metabolism, Physiology