Molecular chaperone functions in protein folding and proteostasis.

By Yujin E. Kim, M. Hipp, A. Bracher, M. Hayer-Hartl, F. Hartl. Annual Review of Biochemistry, 2013

1,454 citations recorded by the source corpus.

The biological functions of proteins are governed by their three-dimensional fold. Protein folding, maintenance of proteome integrity, and protein homeostasis (proteostasis) critically depend on a complex network of molecular chaperones. Disruption of proteostasis is implicated in aging and the pathogenesis of numerous degenerative diseases. In the cytosol, different classes of molecular chaperones cooperate in evolutionarily conserved folding pathways. Nascent polypeptides interact cotranslationally with a first set of chaperones, including trigger factor and the Hsp70 system, which prevent premature (mis)folding. Folding occurs upon controlled release of newly synthesized proteins from these factors or after transfer to downstream chaperones such as the chaperonins. Chaperonins are large, cylindrical complexes that provide a central compartment for a single protein chain to fold unimpaired by aggregation. This review focuses on recent advances in understanding the mechanisms of chaperone action in promoting and regulating protein folding and on the pathological consequences of protein misfolding and aggregation.

Subfields: Cell Biology, Materials Chemistry, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/b5313cafa17e1168d7764254cabf03637493113c

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Citations in the corpus

In vivo aspects of protein folding and quality control (2016, background): “Several mechanistic paradigms of chaperone function in protein folding have been defined (13).”
Pathways of cellular proteostasis in aging and disease (2018, background): “The PN has previously been proposed to consist of ∼1,000–1,400 components on the basis of our initial understanding of its organization (Balch et al., 2008; Powers et al., 2009; Kim et al., 2013; Hipp et al., 2014).”
The amyloid state and its association with protein misfolding diseases (2014, background): “Paired betasheet structure of an Aβ(1-40) amyloid fibril revealed by electron microscopy.”