Co-chaperones fine-tune the function of heat shock protein 70 (Hsp70), whether to fold, hold, or degrade substrates in ensuring cellular protein homeostasis

Abildgaard AB, Voutsinos V, Petersen SD, et al. 2023 HSP70-binding motifs function as protein quality control degrons. Cell. Mol. Life Sci. 80 32

Article  CAS  PubMed  PubMed Central  Google Scholar 

Abrams JL, Verghese J, Gibney PA, et al. 2014 Hierarchical functional specificity of cytosolic heat shock protein 70 (Hsp70) nucleotide exchange factors in yeast. J. Biol. Chem. 289 13155–13167

Article  CAS  PubMed  PubMed Central  Google Scholar 

Agarraberes FA and Dice JF 2001 A molecular chaperone complex at the lysosomal membrane is required for protein translocation. J. Cell Sci. 114 2491–2499

Article  CAS  PubMed  Google Scholar 

Albakova Z, Armeev GA, Kanevskiy LM, et al. 2020 HSP70 multi-functionality in cancer. Cells 9 587

Article  CAS  PubMed  PubMed Central  Google Scholar 

Andersson R, Eisele-Burger AM, Hanzen S, et al. 2021 Differential role of cytosolic Hsp70s in longevity assurance and protein quality control. PLoS Genet. 17 e1008951

Article  CAS  PubMed  PubMed Central  Google Scholar 

Andreasson C, Fiaux J, Rampelt H, et al. 2008 Insights into the structural dynamics of the Hsp110-Hsp70 interaction reveal the mechanism for nucleotide exchange activity. Proc. Natl. Acad. Sci. USA 105 16519–16524

Article  CAS  PubMed  PubMed Central  Google Scholar 

Arndt V, Dick N, Tawo R, et al. 2010 Chaperone-assisted selective autophagy is essential for muscle maintenance. Curr. Biol. 20 143–148

Article  CAS  PubMed  Google Scholar 

Bengoechea R, Findlay AR, Bhadra AK, et al. 2020 Inhibition of DNAJ-HSP70 interaction improves strength in muscular dystrophy. J. Clin. Invest. 130 4470–4485

CAS  PubMed  PubMed Central  Google Scholar 

Bhattacharya K and Picard D 2021 The Hsp70-Hsp90 go-between Hop/Stip1/Sti1 is a proteostatic switch and may be a drug target in cancer and neurodegeneration. Cell. Mol. Life Sci. 78 7257–7273

Article  CAS  PubMed  PubMed Central  Google Scholar 

Bhattacharya K, Weidenauer L, Luengo TM, et al. 2020 The Hsp70-Hsp90 co-chaperone Hop/Stip1 shifts the proteostatic balance from folding towards degradation. Nat. Commun. 11 5975

Article  CAS  PubMed  PubMed Central  Google Scholar 

Binder MJ and Pedley AM 2023 The roles of molecular chaperones in regulating cell metabolism. FEBS Lett. 597 1681–1701

Article  CAS  PubMed  PubMed Central  Google Scholar 

Bonini NM 2002 Chaperoning brain degeneration. Proc. Natl. Acad. Sci. USA 99 16407–16411

Article  CAS  PubMed  PubMed Central  Google Scholar 

Boorstein WR, Ziegelhoffer T and Craig EA 1994 Molecular evolution of the HSP70 multigene family. J. Mol. Evol. 38 1–17

Article  CAS  PubMed  Google Scholar 

Boysen M, Kityk R and Mayer MP 2019 Hsp70- and Hsp90-mediated regulation of the conformation of p53 DNA binding domain and p53 cancer variants. Mol. Cell 74 831–843

Article  CAS  PubMed  Google Scholar 

Bracher A and Verghese J 2023 Nucleotide exchange factors for Hsp70 molecular chaperones: GrpE, Hsp110/Grp170, HspBP1/Sil1, and BAG domain proteins. Subcell. Biochem. 101 1–39

Article  CAS  PubMed  Google Scholar 

Buchberger A, Bukau B and Sommer T 2010 Protein quality control in the cytosol and the endoplasmic reticulum: brothers in arms. Mol. Cell. 40 238–252

Article  CAS  PubMed  Google Scholar 

Chiang AN, Liang M, Dominguez-Meijide A, et al. 2019 Synthesis and evaluation of esterified Hsp70 agonists in cellular models of protein aggregation and folding. Bioorg. Med. Chem. 27 79–91

Article  CAS  PubMed  Google Scholar 

Craig EA and Marszalek J 2017 How do J-proteins get Hsp70 to do so many different things? Trends Biochem. Sci. 42 355–368

Article  CAS  PubMed  PubMed Central  Google Scholar 

Das CK, Linder B, Bonn F, et al. 2018 BAG3 overexpression and cytoprotective autophagy mediate apoptosis resistance in chemoresistant breast cancer cells. Neoplasia 20 263–279

Article  CAS  PubMed  PubMed Central  Google Scholar 

de Graff AM, Mosedale DE, Sharp T, et al. 2020 Proteostasis is adaptive: balancing chaperone holdases against foldases. PLoS Comput. Biol. 16 e1008460

Article  PubMed  PubMed Central  Google Scholar 

De Marco M, Turco MC and Marzullo L 2020 BAG3 in tumor resistance to therapy. Trends Cancer 6 985–988

Article  PubMed  Google Scholar 

Escusa-Toret S, Vonk WI and Frydman J 2013 Spatial sequestration of misfolded proteins by a dynamic chaperone pathway enhances cellular fitness during stress. Nat. Cell Biol. 15 1231–1243

Article  CAS  PubMed  PubMed Central  Google Scholar 

Esser C, Scheffner M and Hohfeld J 2005 The chaperone-associated ubiquitin ligase CHIP is able to target p53 for proteasomal degradation. J. Biol. Chem. 280 27443–27448

Article  CAS  PubMed  Google Scholar 

Faust O, Abayev-Avraham M, Wentink AS, et al. 2020 HSP40 proteins use class-specific regulation to drive HSP70 functional diversity. Nature 587 489–494

Article  CAS  PubMed  Google Scholar 

Feder ZA, Ali A, Singh A, et al. 2021 Subcellular localization of the J-protein Sis1 regulates the heat shock response. J. Cell Biol. 220 e202005165

Article  CAS  PubMed  Google Scholar 

Fernandez-Fernandez MR, Gragera M, Ochoa-Ibarrola L, et al. 2017 Hsp70 – a master regulator in protein degradation. FEBS Lett. 591 2648–2660

Article  CAS  PubMed  Google Scholar 

Fernandez-Funez P, Sanchez-Garcia J, de Mena L, et al. 2016 Holdase activity of secreted Hsp70 masks amyloid-beta42 neurotoxicity in Drosophila. Proc. Natl. Acad. Sci. USA 113 E5212–E5221

Article  CAS  PubMed  PubMed Central  Google Scholar 

French JB, Zhao H, An S, et al. 2013 Hsp70/Hsp90 chaperone machinery is involved in the assembly of the purinosome. Proc. Natl. Acad. Sci. USA 110 2528–2533

Article  CAS  PubMed  PubMed Central  Google Scholar 

Frydman J 2001 Folding of newly translated proteins in vivo: the role of molecular chaperones. Annu. Rev. Biochem. 70 603–647

Article  CAS  PubMed  Google Scholar 

Gamerdinger M, Kaya AM, Wolfrum U, et al. 2011 BAG3 mediates chaperone-based aggresome-targeting and selective autophagy of misfolded proteins. EMBO Rep. 12 149–156

Article  CAS  PubMed  PubMed Central

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