Title
Authors
Francesco Piva*, Monia Cecati, Matteo Giulietti
Affiliation
Department of Specialistic Clinical and Odontostomatological Sciences, Polytechnic University of Marche, Monte d'Ago, 60131, Ancona, Italy.
Francesco Piva - E-mail: f.piva@univpm.it; *Corresponding author
Article Type
Editorial
Date
Received December 29, 2019; Accepted December 30, 2019; Published January 1, 2020
Abstract
The heat shock protein Hsp90 is a molecular chaperon that uses ATP and interacts with various co-chaperone proteins, acting as adapters, in order to carry out the maturation of its target proteins. In physiological conditions, the heat shock proteins (HSPs) favour posttranslational modification, protein folding and sub-cellular transport of their “client” proteins. In stress conditions, many misfolded proteins accumulate exposing their hydrophobic residues and these are recognized by HSPs which prevent the aggregation and favour the correct folding. In case this is no longer possible, HSPs mediate elimination of such misfolded proteins, mainly by ubiquitin–proteasome system.
Keywords
Hsp90, regulation, network
Citation
Piva et al. Bioinformation 16(1): 17-20 (2020)
Edited by
P Kangueane
ISSN
0973-2063
Publisher
License
This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.
