Literature DB >> 17441502

All in the family: atypical Hsp70 chaperones are conserved modulators of Hsp70 activity.

Lance Shaner1, Kevin A Morano.   

Abstract

Divergent relatives of the Hsp70 protein chaperone such as the Hsp110 and Grp170 families have been recognized for some time, yet their biochemical roles remained elusive. Recent work has revealed that these "atypical" Hsp70s exist in stable complexes with classic Hsp70s where they exert a powerful nucleotide-exchange activity that synergizes with Hsp40/DnaJ-type cochaperones to dramatically accelerate Hsp70 nucleotide cycling. This represents a novel evolutionary transition from an independent protein-folding chaperone to what appears to be a dedicated cochaperone. Contributions of the atypical Hsp70s to established cellular roles for Hsp70 now must be deciphered.

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Year:  2007        PMID： 17441502      PMCID： PMC1852889          DOI： 10.1379/csc-245r.1

Source DB:  PubMed          Journal:  Cell Stress Chaperones        ISSN： 1355-8145            Impact factor:   3.667


  60 in total

1.  GrpE-like regulation of the hsc70 chaperone by the anti-apoptotic protein BAG-1.

Authors:  J Höhfeld; S Jentsch
Journal:  EMBO J       Date:  1997-10-15       Impact factor: 11.598

Review 2.  The Hsp70 and Hsp60 chaperone machines.

Authors:  B Bukau; A L Horwich
Journal:  Cell       Date:  1998-02-06       Impact factor: 41.582

3.  Functional specificity among Hsp70 molecular chaperones.

Authors:  P James; C Pfund; E A Craig
Journal:  Science       Date:  1997-01-17       Impact factor: 47.728

4.  Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK.

Authors:  C J Harrison; M Hayer-Hartl; M Di Liberto; F Hartl; J Kuriyan
Journal:  Science       Date:  1997-04-18       Impact factor: 47.728

5.  Regulation of transcription factor Pdr1p function by an Hsp70 protein in Saccharomyces cerevisiae.

Authors:  T C Hallstrom; D J Katzmann; R J Torres; W J Sharp; W S Moye-Rowley
Journal:  Mol Cell Biol       Date:  1998-03       Impact factor: 4.272

6.  SSI1 encodes a novel Hsp70 of the Saccharomyces cerevisiae endoplasmic reticulum.

Authors:  B K Baxter; P James; T Evans; E A Craig
Journal:  Mol Cell Biol       Date:  1996-11       Impact factor: 4.272

7.  Nucleotide-induced conformational changes in the ATPase and substrate binding domains of the DnaK chaperone provide evidence for interdomain communication.

Authors:  A Buchberger; H Theyssen; H Schröder; J S McCarty; G Virgallita; P Milkereit; J Reinstein; B Bukau
Journal:  J Biol Chem       Date:  1995-07-14       Impact factor: 5.157

8.  Hsp110 protects heat-denatured proteins and confers cellular thermoresistance.

Authors:  H J Oh; X Chen; J R Subjeck
Journal:  J Biol Chem       Date:  1997-12-12       Impact factor: 5.157

9.  Cer1p, a novel Hsp70-related protein required for posttranslational endoplasmic reticulum translocation in yeast.

Authors:  T G Hamilton; G C Flynn
Journal:  J Biol Chem       Date:  1996-11-29       Impact factor: 5.157

10.  The 170 kDa glucose regulated stress protein is a large HSP70-, HSP110-like protein of the endoplasmic reticulum.

Authors:  X Chen; D Easton; H J Oh; D S Lee-Yoon; X Liu; J Subjeck
Journal:  FEBS Lett       Date:  1996-02-12       Impact factor: 4.124
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  52 in total

1.  Unique peptide substrate binding properties of 110-kDa heat-shock protein (Hsp110) determine its distinct chaperone activity.

Authors:  Xinping Xu; Evans Boateng Sarbeng; Christina Vorvis; Divya Prasanna Kumar; Lei Zhou; Qinglian Liu
Journal:  J Biol Chem       Date:  2011-12-08       Impact factor: 5.157

Review 2.  The delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiology.

Authors:  Christopher J Guerriero; Jeffrey L Brodsky
Journal:  Physiol Rev       Date:  2012-04       Impact factor: 37.312

3.  J domain co-chaperone specificity defines the role of BiP during protein translocation.

Authors:  Shruthi S Vembar; Martin C Jonikas; Linda M Hendershot; Jonathan S Weissman; Jeffrey L Brodsky
Journal:  J Biol Chem       Date:  2010-04-29       Impact factor: 5.157

Review 4.  The endoplasmic reticulum protein folding factory and its chaperones: new targets for drug discovery?

Authors:  Martin McLaughlin; Koen Vandenbroeck
Journal:  Br J Pharmacol       Date:  2011-01       Impact factor: 8.739

5.  Blocking Hsp70 enhances the efficiency of amphotericin B treatment against resistant Aspergillus terreus strains.

Authors:  Michael Blatzer; Gerhard Blum; Emina Jukic; Wilfried Posch; Peter Gruber; Markus Nagl; Ulrike Binder; Elisabeth Maurer; Bettina Sarg; Herbert Lindner; Cornelia Lass-Flörl; Doris Wilflingseder
Journal:  Antimicrob Agents Chemother       Date:  2015-04-13       Impact factor: 5.191

Review 6.  Heat shock protein 70 (hsp70) as an emerging drug target.

Authors:  Christopher G Evans; Lyra Chang; Jason E Gestwicki
Journal:  J Med Chem       Date:  2010-06-24       Impact factor: 7.446

Review 7.  The activities and function of molecular chaperones in the endoplasmic reticulum.

Authors:  Teresa M Buck; Christine M Wright; Jeffrey L Brodsky
Journal:  Semin Cell Dev Biol       Date:  2007-09-08       Impact factor: 7.727

8.  The large Hsp70 Grp170 binds to unfolded protein substrates in vivo with a regulation distinct from conventional Hsp70s.

Authors:  Julia Behnke; Linda M Hendershot
Journal:  J Biol Chem       Date:  2013-12-10       Impact factor: 5.157

Review 9.  Chaperome Networks - Redundancy and Implications for Cancer Treatment.

Authors:  Pengrong Yan; Tai Wang; Monica L Guzman; Radu I Peter; Gabriela Chiosis
Journal:  Adv Exp Med Biol       Date:  2020       Impact factor: 2.622

10.  Heteromeric complexes of heat shock protein 70 (HSP70) family members, including Hsp70B', in differentiated human neuronal cells.

Authors:  Ari M Chow; Philip Mok; Dawn Xiao; Sam Khalouei; Ian R Brown
Journal:  Cell Stress Chaperones       Date:  2010-01-19       Impact factor: 3.667
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