Chaperone families and interactions in metazoa

Citations Over TimeTop 10% of 2016 papers

Abstract

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.

Related Papers

• → Unfolding the role of chaperones and chaperonins in human disease(2001)119 cited
• → Disease-Associated Mutations in the HSPD1 Gene Encoding the Large Subunit of the Mitochondrial HSP60/HSP10 Chaperonin Complex(2016)58 cited
• → Hsp60 Friend and Foe of the Nervous System(2019)2 cited
• → Function of the maize mitochondrial chaperonin hsp60: specific association between hsp60 and newly synthesized F1-ATPase alpha subunits.(1990)59 cited
• → Function of the Maize Mitochondrial Chaperonin hsp60: Specific Association between hsp60 and Newly Synthesized F1-ATPase Alpha Subunits(1990)17 cited