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Hsp70 – a master regulator in protein degradation
Author(s) -
FernándezFernández María Rosario,
Gragera Marcos,
OchoaIbarrola Lissette,
QuintanaGallardo Lucía,
Valpuesta José María
Publication year - 2017
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12751
Subject(s) - proteostasis , protein folding , microbiology and biotechnology , proteasome , protein degradation , autophagy , chaperone (clinical) , regulator , ubiquitin , hsp70 , context (archaeology) , endoplasmic reticulum associated protein degradation , biology , protein aggregation , heat shock protein , unfolded protein response , biochemistry , endoplasmic reticulum , apoptosis , paleontology , medicine , pathology , gene
Proteostasis, the controlled balance of protein synthesis, folding, assembly, trafficking and degradation, is a paramount necessity for cell homeostasis. Impaired proteostasis is a hallmark of ageing and of many human diseases. Molecular chaperones are essential for proteostasis in eukaryotic cells, and their function has traditionally been linked to protein folding, assembly and disaggregation. More recent findings suggest that chaperones also contribute to key steps in protein degradation. In particular, Hsp70 has an essential role in substrate degradation through the ubiquitin–proteasome system, as well as through different autophagy pathways. Accumulated knowledge suggests that the fate of an Hsp70 substrate is dictated by the combination of partners (cochaperones and other chaperones) that interact with Hsp70 in a given cell context.