HSP40 proteins use class-specific regulation to drive HSP70 functional diversity

• Published in: Nature (London) Vol. 587; no. 7834; pp. 489 - 494
• Main Authors: Faust, Ofrah, Abayev-Avraham, Meital, Wentink, Anne S., Maurer, Michael, Nillegoda, Nadinath B., London, Nir, Bukau, Bernd, Rosenzweig, Rina
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 19.11.2020; Nature Publishing Group
• Subjects: alpha-Synuclein - chemistry; alpha-Synuclein - metabolism; Amyloid - chemistry; Amyloid - metabolism; Binding Sites; Chaperones; Disaggregation; Fibers; Glycine; Glycine - metabolism; Health aspects; Heat shock proteins; HSP40 Heat-Shock Proteins - chemistry; HSP40 Heat-Shock Proteins - metabolism; Hsp40 protein; HSP70 Heat-Shock Proteins - chemistry; HSP70 Heat-Shock Proteins - genetics; HSP70 Heat-Shock Proteins - metabolism; Hsp70 protein; Humanities and Social Sciences; Humans; Life cycles; Magnetic resonance; Molecular Chaperones - chemistry; Molecular Chaperones - metabolism; multidisciplinary; Mutation; NMR; Nuclear magnetic resonance; Phenylalanine; Phenylalanine - metabolism; Protein Aggregates; Protein Aggregation, Pathological; Protein Binding - genetics; Protein biosynthesis; Protein Domains; Proteins; Science; Science (multidisciplinary); Selectivity; Sequence Deletion; Spectrum analysis; Substrate Specificity; Substrates; Israel

The ubiquitous heat shock protein 70 (HSP70) family consists of ATP-dependent molecular chaperones, which perform numerous cellular functions that affect almost all aspects of the protein life cycle from synthesis to degradation 1 – 3 . Achieving this broad spectrum of functions requires precise reg...