Chaperone families and interactions in metazoa.
Quality control is an essential aspect of cellular function, with protein folding quality control being carried out by molecular chaperones, a diverse group of highly conserved proteins that specifically identify misfolded conformations. Molecular chaperones are thus required to support proteins affected by expressed polymorphisms, mutations, intrinsic errors in gene expression, chronic insult or the acute effects of the environment, all of which contribute to a flux of metastable proteins. In this article, we review the four main chaperone families in metazoans, namely Hsp60 (where Hsp is heat-shock protein), Hsp70, Hsp90 and sHsps (small heat-shock proteins), as well as their co-chaperones. Specifically, we consider the structural and functional characteristics of each family and discuss current models that attempt to explain how chaperones recognize and act together to protect or recover aberrant proteins.
['Bar-Lavan|Yael|Y|', 'Shemesh|Netta|N|', 'Ben-Zvi|Anat|A|']
D000818:Animals D008954:Models, Biological D018832:Molecular Chaperones D005810:Multigene Family D011485:Protein Binding D060066:Protein Interaction Maps
chaperone folding Hsp60 Hsp70 Hsp90 sHsp C. elegans Hsp100 heat shock proteins (Hsp) proteostasis