Gaining new insights on the Hsp90 regulatory network

Francesco Piva; Monia Cecati; Matteo Giulietti

doi:10.6026/97320630016017

Gaining new insights on the Hsp90 regulatory network

Bioinformation. 2020 Jan 1;16(1):17-20. doi: 10.6026/97320630016017. eCollection 2020.

Authors

Francesco Piva¹, Monia Cecati¹, Matteo Giulietti¹

Affiliation

¹ Department of Specialistic Clinical and Odontostomatological Sciences, Polytechnic University of Marche, Monte d'Ago, 60131, Ancona, Italy.

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 post-translational 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; network; regulation.

Publication types

Editorial