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PMID: 20651708 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Review

The HSP70 chaperone machinery: J proteins as drivers of functional specificity.

Nature reviews. Molecular cell biology ·Vol. 11 ·No. 8 ·2010-08-00 ·Pages 579-92

Kampinga HH, Craig EA

Abstract

Heat shock 70 kDa proteins (HSP70s) are ubiquitous molecular chaperones that function in a myriad of biological processes, modulating polypeptide folding, degradation and translocation across membranes, and protein-protein interactions. This multitude of roles is not easily reconciled with the universality of the activity of HSP70s in ATP-dependent client protein-binding and release cycles. Much of the functional diversity of the HSP70s is driven by a diverse class of cofactors: J proteins. Often, multiple J proteins function with a single HSP70. Some target HSP70 activity to clients at precise locations in cells and others bind client proteins directly, thereby delivering specific clients to HSP70 and directly determining their fate.

MeSH Terms
Adenosine Triphosphate/metabolism Guanine Nucleotide Exchange Factors/chemistry,metabolism HSP40 Heat-Shock Proteins/chemistry,metabolism HSP70 Heat-Shock Proteins/chemistry,metabolism Humans Models, Biological Models, Molecular Protein Binding Protein Folding Protein Interaction Domains and Motifs Saccharomyces cerevisiae Proteins/chemistry,metabolism
Chemicals
Guanine Nucleotide Exchange Factors HSP40 Heat-Shock Proteins HSP70 Heat-Shock Proteins Saccharomyces cerevisiae Proteins Adenosine Triphosphate
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Kampinga Harm H
Department of Cell Biology, University of Groningen, University Medical Center, 713 AV Groningen, The Netherlands. [email protected]
Craig Elizabeth A
References (142)
142 references, click to expand
  1. Ubiquitylation of BAG-1 suggests a novel regulatory mechanism during the sorting of chaperone substrates to the proteasome.
    J Biol Chem. 2002 Nov 29;277(48):45920-7 PMID: 12297498
  2. Function of trigger factor and DnaK in multidomain protein folding: increase in yield at the expense of folding speed.
    Cell. 2004 Apr 16;117(2):199-209 PMID: 15084258
  3. Interaction of the J-protein heterodimer Pam18/Pam16 of the mitochondrial import motor with the translocon of the inner membrane.
    Mol Biol Cell. 2008 Jan;19(1):424-32 PMID: 18003975
  4. The crystal structure of the yeast Hsp40 Ydj1 complexed with its peptide substrate.
    Structure. 2003 Dec;11(12):1475-83 PMID: 14656432
  5. LHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulum.
    EMBO J. 2000 Dec 1;19(23):6440-52 PMID: 11101517
  6. Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding.
    Cell. 2008 Jun 13;133(6):1068-79 PMID: 18555782
  7. The interplay between components of the mitochondrial protein translocation motor studied using purified components.
    J Biol Chem. 2007 Nov 23;282(47):33935-42 PMID: 17881357
  8. Cwc23, an essential J protein critical for pre-mRNA splicing with a dispensable J domain.
    Mol Cell Biol. 2010 Jan;30(1):33-42 PMID: 19822657
  9. Residues of Tim44 involved in both association with the translocon of the inner mitochondrial membrane and regulation of mitochondrial Hsp70 tethering.
    Mol Cell Biol. 2008 Jul;28(13):4424-33 PMID: 18426906
  10. Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation.
    Cell. 2000 Apr 28;101(3):249-58 PMID: 10847680
  11. Characterization of Hsp70 binding and nucleotide exchange by the yeast Hsp110 chaperone Sse1.
    Biochemistry. 2006 Dec 19;45(50):15075-84 PMID: 17154545
  12. Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function.
    Cell Stress Chaperones. 1998 Mar;3(1):28-36 PMID: 9585179
  13. Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s.
    EMBO J. 2006 Jun 7;25(11):2519-28 PMID: 16688212
  14. The roles of the two zinc binding sites in DnaJ.
    J Biol Chem. 2003 Nov 7;278(45):44457-66 PMID: 12941935
  15. Dissociation of clathrin coats coupled to the hydrolysis of ATP: role of an uncoating ATPase.
    J Cell Biol. 1984 Aug;99(2):734-41 PMID: 6146631
  16. JPDI, a novel endoplasmic reticulum-resident protein containing both a BiP-interacting J-domain and thioredoxin-like motifs.
    J Biol Chem. 2003 Jan 24;278(4):2669-76 PMID: 12446677
  17. Modulation of in vivo HSP70 chaperone activity by Hip and Bag-1.
    J Biol Chem. 2001 Feb 16;276(7):4677-82 PMID: 11076956
  18. Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate.
    Proc Natl Acad Sci U S A. 2009 May 26;106(21):8471-6 PMID: 19439666
  19. The crystal structure of the C-terminal fragment of yeast Hsp40 Ydj1 reveals novel dimerization motif for Hsp40.
    J Mol Biol. 2005 Mar 4;346(4):1005-11 PMID: 15701512
  20. The crystal structure of the peptide-binding fragment from the yeast Hsp40 protein Sis1.
    Structure. 2000 Aug 15;8(8):799-807 PMID: 10997899
  21. Hsp40 molecules that target to the ubiquitin-proteasome system decrease inclusion formation in models of polyglutamine disease.
    Mol Ther. 2007 Jun;15(6):1100-5 PMID: 17426712
  22. Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p.
    Mol Cell Biol. 2002 Jul;22(13):4677-89 PMID: 12052876
  23. The Hsp40 chaperone Jjj1 is required for the nucleo-cytoplasmic recycling of preribosomal factors in Saccharomyces cerevisiae.
    RNA. 2007 Sep;13(9):1570-81 PMID: 17652132
  24. The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation.
    Nat Cell Biol. 2001 Jan;3(1):100-5 PMID: 11146634
  25. Role of the J-domain in the cooperation of Hsp40 with Hsp70.
    Proc Natl Acad Sci U S A. 1998 May 26;95(11):6108-13 PMID: 9600925
  26. The chaperoning activity of hsp110. Identification of functional domains by use of targeted deletions.
    J Biol Chem. 1999 May 28;274(22):15712-8 PMID: 10336470
  27. Hsp70 and Hsp40 chaperone activities in the cytoplasm and the nucleus of mammalian cells.
    J Biol Chem. 1997 Dec 26;272(52):33283-9 PMID: 9407119
  28. Bag-1M accelerates nucleotide release for human Hsc70 and Hsp70 and can act concentration-dependent as positive and negative cofactor.
    J Biol Chem. 2001 Aug 31;276(35):32538-44 PMID: 11441021
  29. Modulation of polyglutamine inclusion formation by the Hsp70 chaperone machine.
    Exp Cell Res. 2007 Oct 1;313(16):3568-78 PMID: 17822698
  30. Swapping nucleotides, tuning Hsp70.
    Cell. 2008 Jun 13;133(6):945-7 PMID: 18555768
  31. Genetic suppression of polyglutamine toxicity in Drosophila.
    Science. 2000 Mar 10;287(5459):1837-40 PMID: 10710314
  32. ERdj3, a stress-inducible endoplasmic reticulum DnaJ homologue, serves as a cofactor for BiP's interactions with unfolded substrates.
    Mol Biol Cell. 2005 Jan;16(1):40-50 PMID: 15525676
  33. Dimeric novel HSP40 is incorporated into the radial spoke complex during the assembly process in flagella.
    Mol Biol Cell. 2005 Feb;16(2):637-48 PMID: 15563613
  34. Mitochondrial GrpE modulates the function of matrix Hsp70 in translocation and maturation of preproteins.
    Mol Cell Biol. 1995 Dec;15(12):7098-105 PMID: 8524277
  35. Specificity of the J-protein Sis1 in the propagation of 3 yeast prions.
    Proc Natl Acad Sci U S A. 2008 Oct 28;105(43):16596-601 PMID: 18955697
  36. Neuronal DnaJ proteins HSJ1a and HSJ1b: a role in linking the Hsp70 chaperone machine to the ubiquitin-proteasome system?
    Biochem Soc Trans. 2004 Aug;32(Pt 4):640-2 PMID: 15270696
  37. The role of the DIF motif of the DnaJ (Hsp40) co-chaperone in the regulation of the DnaK (Hsp70) chaperone cycle.
    J Biol Chem. 2006 May 5;281(18):12436-44 PMID: 16533811
  38. Chaperone functions of the E3 ubiquitin ligase CHIP.
    J Biol Chem. 2007 Aug 3;282(31):22267-77 PMID: 17545168
  39. Chaperoned ubiquitylation--crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex.
    Mol Cell. 2005 Nov 23;20(4):525-38 PMID: 16307917
  40. Human Mpp11 J protein: ribosome-tethered molecular chaperones are ubiquitous.
    Science. 2005 May 13;308(5724):1032-4 PMID: 15802566
  41. The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins.
    Nat Cell Biol. 2001 Jan;3(1):93-6 PMID: 11146632
  42. The role of the GrpE homologue, Mge1p, in mediating protein import and protein folding in mitochondria.
    EMBO J. 1995 Jul 17;14(14):3452-60 PMID: 7628446
  43. Allosteric regulation of Hsp70 chaperones involves a conserved interdomain linker.
    J Biol Chem. 2006 Dec 15;281(50):38705-11 PMID: 17052976
  44. Analysis of the levels of conservation of the J domain among the various types of DnaJ-like proteins.
    Cell Stress Chaperones. 2000 Oct;5(4):347-58 PMID: 11048657
  45. Characterization of the interaction between the J-protein Jac1p and the scaffold for Fe-S cluster biogenesis, Isu1p.
    J Biol Chem. 2006 May 26;281(21):14580-7 PMID: 16551614
  46. Crystal structure of Hsc20, a J-type Co-chaperone from Escherichia coli.
    J Mol Biol. 2000 Dec 15;304(5):835-45 PMID: 11124030
  47. Allosteric regulation of Hsp70 chaperones by a proline switch.
    Mol Cell. 2006 Feb 3;21(3):359-67 PMID: 16455491
  48. Hsp70 chaperones: cellular functions and molecular mechanism.
    Cell Mol Life Sci. 2005 Mar;62(6):670-84 PMID: 15770419
  49. Structure of the Hsp110:Hsc70 nucleotide exchange machine.
    Mol Cell. 2008 Jul 25;31(2):232-43 PMID: 18550409
  50. Chaperone-dependent E3 ubiquitin ligase CHIP mediates a degradative pathway for c-ErbB2/Neu.
    Proc Natl Acad Sci U S A. 2002 Oct 1;99(20):12847-52 PMID: 12239347
  51. Bag1 functions in vivo as a negative regulator of Hsp70 chaperone activity.
    Mol Cell Biol. 2000 Feb;20(3):1083-8 PMID: 10629065
  52. ERdj5, an endoplasmic reticulum (ER)-resident protein containing DnaJ and thioredoxin domains, is expressed in secretory cells or following ER stress.
    J Biol Chem. 2003 Jan 10;278(2):1059-66 PMID: 12411443
  53. Molecular chaperones enhance the degradation of expanded polyglutamine repeat androgen receptor in a cellular model of spinal and bulbar muscular atrophy.
    Hum Mol Genet. 2002 Mar 1;11(5):515-23 PMID: 11875046
  54. Cardioprotective effects of 70-kDa heat shock protein in transgenic mice.
    Proc Natl Acad Sci U S A. 1996 Mar 19;93(6):2339-42 PMID: 8637874
  55. Farnesylation of YDJ1p is required for function at elevated growth temperatures in Saccharomyces cerevisiae.
    J Biol Chem. 1992 Sep 15;267(26):18890-5 PMID: 1527016
  56. Mutational analysis of the hsp70-interacting protein Hip.
    Mol Cell Biol. 1996 Nov;16(11):6200-7 PMID: 8887650
  57. Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains.
    Cell. 1999 Jun 11;97(6):755-65 PMID: 10380927
  58. Molecular chaperones and protein quality control.
    Cell. 2006 May 5;125(3):443-51 PMID: 16678092
  59. Specificity of class II Hsp40 Sis1 in maintenance of yeast prion [RNQ+].
    Mol Biol Cell. 2003 Mar;14(3):1172-81 PMID: 12631732
  60. Chaperones in control of protein disaggregation.
    EMBO J. 2008 Jan 23;27(2):328-35 PMID: 18216875
  61. Heat shock protein 70 chaperone overexpression ameliorates phenotypes of the spinal and bulbar muscular atrophy transgenic mouse model by reducing nuclear-localized mutant androgen receptor protein.
    J Neurosci. 2003 Mar 15;23(6):2203-11 PMID: 12657679
  62. Molecular model for a complete clathrin lattice from electron cryomicroscopy.
    Nature. 2004 Dec 2;432(7017):573-9 PMID: 15502812
  63. Importing mitochondrial proteins: machineries and mechanisms.
    Cell. 2009 Aug 21;138(4):628-44 PMID: 19703392
  64. Temperature-controlled activity of DnaK-DnaJ-GrpE chaperones: protein-folding arrest and recovery during and after heat shock depends on the substrate protein and the GrpE concentration.
    Biochemistry. 1998 Jul 7;37(27):9688-94 PMID: 9657681
  65. Overexpression of the cochaperone CHIP enhances Hsp70-dependent folding activity in mammalian cells.
    Mol Cell Biol. 2003 Jul;23(14):4948-58 PMID: 12832480
  66. Proteins as molecular chaperones.
    Nature. 1987 Jul 30-Aug 5;328(6129):378-9 PMID: 3112578
  67. Guidelines for the nomenclature of the human heat shock proteins.
    Cell Stress Chaperones. 2009 Jan;14(1):105-11 PMID: 18663603
  68. NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone.
    J Mol Biol. 1996 Jul 12;260(2):236-50 PMID: 8764403
  69. Isolation and characterization of SSE1 and SSE2, new members of the yeast HSP70 multigene family.
    Gene. 1993 Sep 30;132(1):57-66 PMID: 8406043
  70. Association of the Tim14.Tim16 subcomplex with the TIM23 translocase is crucial for function of the mitochondrial protein import motor.
    J Biol Chem. 2007 Jun 22;282(25):18037-18045 PMID: 17452317
  71. HspB8 participates in protein quality control by a non-chaperone-like mechanism that requires eIF2{alpha} phosphorylation.
    J Biol Chem. 2009 Feb 27;284(9):5523-32 PMID: 19114712
  72. Eradication of glioblastoma, and breast and colon carcinoma xenografts by Hsp70 depletion.
    Cancer Res. 2002 Dec 15;62(24):7139-42 PMID: 12499245
  73. A motif in the clathrin heavy chain required for the Hsc70/auxilin uncoating reaction.
    Mol Biol Cell. 2008 Jan;19(1):405-13 PMID: 17978091
  74. HSJ1 is a neuronal shuttling factor for the sorting of chaperone clients to the proteasome.
    Curr Biol. 2005 Jun 7;15(11):1058-64 PMID: 15936278
  75. HscA and HscB stimulate [2Fe-2S] cluster transfer from IscU to apoferredoxin in an ATP-dependent reaction.
    Biochemistry. 2006 Sep 19;45(37):11087-95 PMID: 16964969
  76. Mammalian HSP40/DNAJ homologs: cloning of novel cDNAs and a proposal for their classification and nomenclature.
    Cell Stress Chaperones. 2000 Apr;5(2):98-112 PMID: 11147971
  77. The mitochondrial proteins Ssq1 and Jac1 are required for the assembly of iron sulfur clusters in mitochondria.
    J Mol Biol. 2001 Mar 30;307(3):815-25 PMID: 11273703
  78. The translation machinery and 70 kd heat shock protein cooperate in protein synthesis.
    Cell. 1992 Oct 2;71(1):97-105 PMID: 1394434
  79. The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE.
    Proc Natl Acad Sci U S A. 1994 Oct 25;91(22):10345-9 PMID: 7937953
  80. Overexpression of heat shock protein 70 in R6/2 Huntington's disease mice has only modest effects on disease progression.
    Brain Res. 2003 Apr 25;970(1-2):47-57 PMID: 12706247
  81. The diverse roles of J-proteins, the obligate Hsp70 co-chaperone.
    Rev Physiol Biochem Pharmacol. 2006;156:1-21 PMID: 16634144
  82. Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli.
    Cell. 2005 Jul 29;122(2):209-20 PMID: 16051146
  83. A DNAJB chaperone subfamily with HDAC-dependent activities suppresses toxic protein aggregation.
    Mol Cell. 2010 Feb 12;37(3):355-69 PMID: 20159555
  84. HspB8 chaperone activity toward poly(Q)-containing proteins depends on its association with Bag3, a stimulator of macroautophagy.
    J Biol Chem. 2008 Jan 18;283(3):1437-1444 PMID: 18006506
  85. Hsp70 chaperone ligands control domain association via an allosteric mechanism mediated by the interdomain linker.
    Mol Cell. 2007 Apr 13;26(1):27-39 PMID: 17434124
  86. Dimeric heat shock protein 40 binds radial spokes for generating coupled power strokes and recovery strokes of 9 + 2 flagella.
    J Cell Biol. 2008 Jan 28;180(2):403-15 PMID: 18227282
  87. Initiation of lambda DNA replication with purified host- and bacteriophage-encoded proteins: the role of the dnaK, dnaJ and grpE heat shock proteins.
    EMBO J. 1989 May;8(5):1601-8 PMID: 2527744
  88. The cytosolic J-protein, Jjj1, and Rei1 function in the removal of the pre-60 S subunit factor Arx1.
    J Biol Chem. 2010 Jan 8;285(2):961-8 PMID: 19901025
  89. Inhibition of a spliceosome turnover pathway suppresses splicing defects.
    Proc Natl Acad Sci U S A. 2006 Sep 12;103(37):13700-5 PMID: 16945917
  90. Solution structure of the iron-sulfur cluster cochaperone HscB and its binding surface for the iron-sulfur assembly scaffold protein IscU.
    Biochemistry. 2008 Sep 9;47(36):9394-404 PMID: 18702525
  91. The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasome.
    J Biol Chem. 2000 Feb 18;275(7):4613-7 PMID: 10671488
  92. Jac1, a mitochondrial J-type chaperone, is involved in the biogenesis of Fe/S clusters in Saccharomyces cerevisiae.
    Proc Natl Acad Sci U S A. 2001 Feb 13;98(4):1483-8 PMID: 11171977
  93. Molecular chaperones HscA/Ssq1 and HscB/Jac1 and their roles in iron-sulfur protein maturation.
    Crit Rev Biochem Mol Biol. 2007 Mar-Apr;42(2):95-111 PMID: 17453917
  94. Identification of a consensus motif in substrates bound by a Type I Hsp40.
    Proc Natl Acad Sci U S A. 2009 Jul 7;106(27):11073-8 PMID: 19549854
  95. Genetic and biochemical characterization of mutations affecting the carboxy-terminal domain of the Escherichia coli molecular chaperone DnaJ.
    Mol Microbiol. 1998 Oct;30(2):329-40 PMID: 9791178
  96. Chaperones get Hip. Protein folding.
    Curr Biol. 1996 Mar 1;6(3):272-5 PMID: 8805243
  97. Farnesylation of Ydj1 is required for in vivo interaction with Hsp90 client proteins.
    Mol Biol Cell. 2008 Dec;19(12):5249-58 PMID: 18829866
  98. Some like it hot: the structure and function of small heat-shock proteins.
    Nat Struct Mol Biol. 2005 Oct;12(10):842-6 PMID: 16205709
  99. The heat shock protein 70 cochaperone hip enhances functional maturation of glucocorticoid receptor.
    Mol Endocrinol. 2004 Jul;18(7):1620-30 PMID: 15071092
  100. Interaction of Kar2p and Sls1p is required for efficient co-translational translocation of secreted proteins in the yeast Yarrowia lipolytica.
    J Biol Chem. 1998 Nov 20;273(47):30903-8 PMID: 9812983
  101. The Hsp90 chaperone machinery.
    J Biol Chem. 2008 Jul 4;283(27):18473-7 PMID: 18442971
  102. The Hsp70 Ssz1 modulates the function of the ribosome-associated J-protein Zuo1.
    Nat Struct Mol Biol. 2005 Jun;12(6):497-504 PMID: 15908962
  103. Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor.
    EMBO J. 2006 Jun 7;25(11):2510-8 PMID: 16688211
  104. Network of general and specialty J protein chaperones of the yeast cytosol.
    Proc Natl Acad Sci U S A. 2007 Apr 24;104(17):7163-8 PMID: 17438278
  105. Studies on the mechanism of catalysis of iron-sulfur cluster transfer from IscU[2Fe2S] by HscA/HscB chaperones.
    Biochemistry. 2008 Dec 2;47(48):12795-801 PMID: 18986169
  106. Visualization of the binding of Hsc70 ATPase to clathrin baskets: implications for an uncoating mechanism.
    J Biol Chem. 2005 Feb 25;280(8):7156-61 PMID: 15596443
  107. Minireview: the intersection of steroid receptors with molecular chaperones: observations and questions.
    Mol Endocrinol. 2008 Oct;22(10):2229-40 PMID: 18451092
  108. Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries.
    EMBO J. 1997 Apr 1;16(7):1501-7 PMID: 9130695
  109. Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions.
    Mol Cell Biol. 1999 Jun;19(6):4535-45 PMID: 10330192
  110. ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER.
    Science. 2008 Jul 25;321(5888):569-72 PMID: 18653895
  111. Molecular chaperones: proteins essential for the biogenesis of some macromolecular structures.
    Trends Biochem Sci. 1989 Aug;14(8):339-42 PMID: 2572080
  112. Overexpression of the rat inducible 70-kD heat stress protein in a transgenic mouse increases the resistance of the heart to ischemic injury.
    J Clin Invest. 1995 Apr;95(4):1446-56 PMID: 7706448
  113. The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated complex.
    Proc Natl Acad Sci U S A. 2005 Jul 19;102(29):10064-9 PMID: 16002468
  114. The Hsp70 chaperone Ssq1p is dispensable for iron-sulfur cluster formation on the scaffold protein Isu1p.
    J Biol Chem. 2006 Mar 24;281(12):7801-8 PMID: 16431909
  115. Interaction of the Hsp70 molecular chaperone, DnaK, with its cochaperone DnaJ.
    Proc Natl Acad Sci U S A. 1998 Dec 22;95(26):15223-8 PMID: 9860950
  116. Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones.
    Proc Natl Acad Sci U S A. 1999 May 11;96(10):5452-7 PMID: 10318904
  117. Mutations in the DnaK chaperone affecting interaction with the DnaJ cochaperone.
    Proc Natl Acad Sci U S A. 1998 Dec 22;95(26):15229-34 PMID: 9860951
  118. DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage.
    EMBO J. 1993 Nov;12(11):4137-44 PMID: 7900997
  119. The conserved carboxyl terminus and zinc finger-like domain of the co-chaperone Ydj1 assist Hsp70 in protein folding.
    J Biol Chem. 1998 Mar 6;273(10):5970-8 PMID: 9488737
  120. Characterization of a brain-enriched chaperone, MRJ, that inhibits Huntingtin aggregation and toxicity independently.
    J Biol Chem. 2002 May 31;277(22):19831-8 PMID: 11896048
  121. Converging concepts of protein folding in vitro and in vivo.
    Nat Struct Mol Biol. 2009 Jun;16(6):574-81 PMID: 19491934
  122. Regulated release of ERdj3 from unfolded proteins by BiP.
    EMBO J. 2008 Nov 5;27(21):2873-82 PMID: 18923428
  123. A Drosophila ortholog of the human MRJ modulates polyglutamine toxicity and aggregation.
    Neurobiol Dis. 2006 Nov;24(2):226-44 PMID: 16934481
  124. Dissecting the ER-associated degradation of a misfolded polytopic membrane protein.
    Cell. 2008 Jan 11;132(1):101-12 PMID: 18191224
  125. The role of ATP in the functional cycle of the DnaK chaperone system.
    J Mol Biol. 1995 May 26;249(1):126-37 PMID: 7776367
  126. Zuotin, a ribosome-associated DnaJ molecular chaperone.
    EMBO J. 1998 Aug 17;17(16):4809-17 PMID: 9707440
  127. Over-expression of inducible HSP70 chaperone suppresses neuropathology and improves motor function in SCA1 mice.
    Hum Mol Genet. 2001 Jul 1;10(14):1511-8 PMID: 11448943
  128. Spp382p interacts with multiple yeast splicing factors, including possible regulators of Prp43 DExD/H-Box protein function.
    Genetics. 2009 Sep;183(1):195-206 PMID: 19581443
  129. Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle.
    Cell. 1995 Nov 17;83(4):589-98 PMID: 7585962
  130. Molecular chaperone targeting and regulation by BAG family proteins.
    Nat Cell Biol. 2001 Oct;3(10):E237-41 PMID: 11584289
  131. Structural basis of J cochaperone binding and regulation of Hsp70.
    Mol Cell. 2007 Nov 9;28(3):422-33 PMID: 17996706
  132. An essential role for the substrate-binding region of Hsp40s in Saccharomyces cerevisiae.
    J Cell Biol. 2001 Feb 19;152(4):851-6 PMID: 11266475
  133. Multiple interactions of auxilin 1 with clathrin and the AP-2 adaptor complex.
    J Biol Chem. 2001 Sep 28;276(39):36131-8 PMID: 11470803
  134. Escherichia coli grpE gene codes for heat shock protein B25.3, essential for both lambda DNA replication at all temperatures and host growth at high temperature.
    J Bacteriol. 1986 Jul;167(1):25-9 PMID: 2424889
  135. The specialized cytosolic J-protein, Jjj1, functions in 60S ribosomal subunit biogenesis.
    Proc Natl Acad Sci U S A. 2007 Jan 30;104(5):1558-63 PMID: 17242366
  136. Structure and dynamics of the iron-sulfur cluster assembly scaffold protein IscU and its interaction with the cochaperone HscB.
    Biochemistry. 2009 Jul 7;48(26):6062-71 PMID: 19492851
  137. Over-expression of hsp70 confers tumorigenicity to mouse fibrosarcoma cells.
    Int J Cancer. 1995 Mar 3;60(5):689-93 PMID: 7860144
  138. Evolution of mitochondrial chaperones utilized in Fe-S cluster biogenesis.
    Curr Biol. 2006 Aug 22;16(16):1660-5 PMID: 16920629
  139. BAP, a mammalian BiP-associated protein, is a nucleotide exchange factor that regulates the ATPase activity of BiP.
    J Biol Chem. 2002 Dec 6;277(49):47557-63 PMID: 12356756
  140. Proteins interacting with the molecular chaperone hsp70/hsc70: physical associations and effects on refolding activity.
    FEBS Lett. 1997 Nov 3;417(1):109-13 PMID: 9395086
  141. Activity of the Hsp70 chaperone complex--DnaK, DnaJ, and GrpE--in initiating phage lambda DNA replication by sequestering and releasing lambda P protein.
    Proc Natl Acad Sci U S A. 1992 Dec 15;89(24):12108-11 PMID: 1361234
  142. Computational analysis of the human HSPH/HSPA/DNAJ family and cloning of a human HSPH/HSPA/DNAJ expression library.
    Cell Stress Chaperones. 2009 Jan;14(1):1-21 PMID: 18686016
Article Info
Journal
Nature reviews. Molecular cell biology
Abbr.
Nat Rev Mol Cell Biol
ISSN
1471-0080
DOI
10.1038/nrm2941
Email
[email protected]
Published
2010-08-00
Pages
579-92
Language
English
Region
England
NLM ID
100962782
PMCID
PMC3003299
Subset
IM
Grants
NIGMS NIH HHS · GM27870 · United States
NIGMS NIH HHS · R01 GM027870 · United States
NIGMS NIH HHS · GM31107 · United States
NIGMS NIH HHS · R01 GM031107 · United States
NIGMS NIH HHS · R01 GM027870-30 · United States
NIGMS NIH HHS · R37 GM031107 · United States
NIGMS NIH HHS · R37 GM031107-27 · United States
NIGMS NIH HHS · R01 GM027870-29 · United States
NIGMS NIH HHS · R37 GM031107-26 · United States
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PubMed source DOI: 10.1038/nrm2941 PMC Full Text View journal details
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