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Dekker SL, Kampinga HH, Bergink S. DNAJs: more than substrate delivery to HSPA. Front Mol Biosci. 2015;2:35doi: 10.3389/fmolb.2015.00035.
Dekker, S. L., Kampinga, H. H., & Bergink, S. (2015). DNAJs: more than substrate delivery to HSPA. Frontiers in molecular biosciences, 235. https://doi.org/10.3389/fmolb.2015.00035
Dekker, Suzanne L, et al. "DNAJs: more than substrate delivery to HSPA." Frontiers in molecular biosciences vol. 2 (2015): 35. doi: https://doi.org/10.3389/fmolb.2015.00035
Dekker SL, Kampinga HH, Bergink S. DNAJs: more than substrate delivery to HSPA. Front Mol Biosci. 2015 Jun 30;2:35. doi: 10.3389/fmolb.2015.00035. eCollection 2015. PMID: 26176011; PMCID: PMC4485348.
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Front Mol Biosci. 2015 Jun 30;2:35. doi: 10.3389/fmolb.2015.00035. eCollection 2015.

DNAJs: more than substrate delivery to HSPA.

Frontiers in molecular biosciences

Suzanne L Dekker, Harm H Kampinga, Steven Bergink

Affiliations

  1. Department of Cell Biology, University Medical Center Groningen, University of Groningen Groningen, Netherlands.

PMID: 26176011 PMCID: PMC4485348 DOI: 10.3389/fmolb.2015.00035

Abstract

Proteins are essential components of cellular life, as building blocks, but also to guide and execute all cellular processes. Proteins require a three-dimensional folding, which is constantly being challenged by their environment. Challenges including elevated temperatures or redox changes can alter this fold and result in misfolding of proteins or even aggregation. Cells are equipped with several pathways that can deal with protein stress. Together, these pathways are referred to as the protein quality control network. The network comprises degradation and (re)folding pathways that are intertwined due to the sharing of components and by the overlap in affinity for substrates. Here, we will give examples of this sharing and intertwinement of protein degradation and protein folding and discuss how the fate of a substrate is determined. We will focus on the ubiquitylation of substrates and the role of Hsp70 co-chaperones of the DNAJ class in this process.

Keywords: DNAJ; HSP70 heat-shock proteins; degradation; protein folding; ubiquitin E3 ligases

References

  1. Cell. 2006 Jan 13;124(1):75-88 - PubMed
  2. Cell. 2008 Jan 11;132(1):101-12 - PubMed
  3. Proc Natl Acad Sci U S A. 2009 May 26;106(21):8471-6 - PubMed
  4. Proc Natl Acad Sci U S A. 2001 Oct 9;98(21):12038-43 - PubMed
  5. Proc Natl Acad Sci U S A. 2009 Sep 1;106(35):14914-9 - PubMed
  6. Nat Rev Mol Cell Biol. 2002 Jun;3(6):411-21 - PubMed
  7. Nat Cell Biol. 2001 Jan;3(1):100-5 - PubMed
  8. Proc Natl Acad Sci U S A. 2013 Mar 26;110(13):5046-51 - PubMed
  9. Trends Mol Med. 2012 Feb;18(2):81-91 - PubMed
  10. Nature. 2010 Dec 23;468(7327):1124-8 - PubMed
  11. Cell. 2004 Jan 23;116(2):221-34 - PubMed
  12. Mol Cell. 2007 Apr 13;26(1):27-39 - PubMed
  13. Curr Biol. 2005 Jun 7;15(11):1058-64 - PubMed
  14. J Biol Chem. 1999 Jul 30;274(31):21943-52 - PubMed
  15. Nucleus. 2011 Nov-Dec;2(6):527-32 - PubMed
  16. Cell. 2012 Nov 21;151(5):1042-54 - PubMed
  17. Elife. 2013 Jan 22;2:e00308 - PubMed
  18. Trends Biochem Sci. 2007 Jan;32(1):6-11 - PubMed
  19. Cell Res. 2011 Mar;21(3):474-85 - PubMed
  20. Nat Rev Mol Cell Biol. 2010 Aug;11(8):579-92 - PubMed
  21. Science. 2006 Jun 23;312(5781):1752-3 - PubMed
  22. Mol Cell. 2001 Jun;7(6):1165-76 - PubMed
  23. Mol Biol Cell. 2011 Feb 1;22(3):301-14 - PubMed
  24. Mol Cell. 2010 Oct 22;40(2):238-52 - PubMed
  25. J Biol Chem. 2007 Sep 7;282(36):26140-9 - PubMed
  26. EMBO J. 2006 Feb 8;25(3):533-43 - PubMed
  27. J Biol Chem. 2000 Feb 18;275(7):4613-7 - PubMed
  28. Mol Biol Cell. 2015 Jan 15;26(2):185-94 - PubMed
  29. Science. 2000 Sep 22;289(5487):2117-20 - PubMed
  30. Sci Signal. 2009 May 26;2(72):ra24 - PubMed
  31. Mol Cell. 2013 May 9;50(3):368-78 - PubMed
  32. Cell. 2013 Jan 17;152(1-2):196-209 - PubMed
  33. Curr Opin Cell Biol. 1992 Apr;4(2):267-73 - PubMed
  34. J Biol Chem. 2009 Apr 17;284(16):10343-52 - PubMed
  35. Cell. 2007 Nov 2;131(3):516-29 - PubMed
  36. Nat Struct Biol. 1999 Jul;6(7):697-705 - PubMed
  37. Cell. 2006 Aug 11;126(3):571-82 - PubMed
  38. PLoS Genet. 2012 Jan;8(1):e1002442 - PubMed
  39. Mol Biol Cell. 2013 Jul;24(13):2076-87 - PubMed
  40. Mol Cell. 2007 Nov 9;28(3):422-33 - PubMed
  41. Annu Rev Biochem. 2006;75:333-66 - PubMed
  42. Mol Biol Cell. 2012 Aug;23(16):3041-56 - PubMed
  43. Cell. 2013 Jul 3;154(1):134-45 - PubMed
  44. EMBO J. 2015 Mar 12;34(6):778-97 - PubMed
  45. Mol Biol Cell. 2010 Jul 1;21(13):2117-27 - PubMed
  46. Genet Eng (N Y). 1999;21:95-111 - PubMed
  47. Nat Rev Mol Cell Biol. 2002 Apr;3(4):246-55 - PubMed
  48. Science. 2010 Aug 13;329(5993):805-10 - PubMed
  49. Nat Cell Biol. 2001 Jan;3(1):93-6 - PubMed
  50. J Clin Invest. 1999 May 15;103(10):1379-89 - PubMed
  51. Science. 2005 May 13;308(5724):1032-4 - PubMed
  52. Annu Rev Biochem. 2013;82:323-55 - PubMed
  53. Methods Mol Biol. 2012;832:455-61 - PubMed
  54. Genes Dev. 2008 Jun 1;22(11):1427-38 - PubMed
  55. Nature. 1994 Jul 14;370(6485):111-7 - PubMed
  56. Cell. 2004 Apr 16;117(2):199-209 - PubMed
  57. Nature. 2011 Jul 20;475(7356):324-32 - PubMed
  58. Structure. 2003 Dec;11(12):1475-83 - PubMed
  59. Proc Natl Acad Sci U S A. 2010 Jan 19;107(3):1106-11 - PubMed

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