Nature's molecular sponges: small heat shock proteins grow into their chaperone roles

doi:10.1073/pnas.0915160107

Comment

. 2010 Feb 16;107(7):2727-8.

doi: 10.1073/pnas.0915160107. Epub 2010 Feb 4.

Nature's molecular sponges: small heat shock proteins grow into their chaperone roles

Stephen J Eyles¹, Lila M Gierasch

Affiliations

PMID: 20133678
PMCID: PMC2840345
DOI: 10.1073/pnas.0915160107

Comment

Nature's molecular sponges: small heat shock proteins grow into their chaperone roles

Stephen J Eyles et al. Proc Natl Acad Sci U S A. 2010.

. 2010 Feb 16;107(7):2727-8.

doi: 10.1073/pnas.0915160107. Epub 2010 Feb 4.

Authors

Stephen J Eyles¹, Lila M Gierasch

Affiliation

¹ Department of Polymer Science and Engineering, University of Massachusetts, Amherst, MA 01003, USA.

PMID: 20133678
PMCID: PMC2840345
DOI: 10.1073/pnas.0915160107

No abstract available

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

**Fig. 1.**
When the native states of proteins (N) become unstable under heat stress, sSHPs passively protect cells against potentially deleterious aggregates by remodeling their oligomeric landscapes. Both increased dissociation of dimeric subunits and a shift to higher oligomeric structures are accompanied by higher affinity for unfolded client molecules (U). The resulting hetero-oligomeric sSHP:client complexes agglomerate into an array of coaggregates that can be recovered by disaggregating Hsp100/Hsp70 chaperone teams.

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Comment on

Quaternary dynamics and plasticity underlie small heat shock protein chaperone function.
Stengel F, Baldwin AJ, Painter AJ, Jaya N, Basha E, Kay LE, Vierling E, Robinson CV, Benesch JL. Stengel F, et al. Proc Natl Acad Sci U S A. 2010 Feb 2;107(5):2007-12. doi: 10.1073/pnas.0910126107. Epub 2010 Jan 19. Proc Natl Acad Sci U S A. 2010. PMID: 20133845 Free PMC article.

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References

1. Hartl FU, Hayer-Hartl M. Converging concepts of protein folding in vitro and in vivo. Nat Struct Mol Biol. 2009;16:574–581. - PubMed
1. Saibil HR. Chaperone machines in action. Curr Opin Struct Biol. 2008;18:35–42. - PubMed
1. Nakamoto H, Vígh L. The small heat shock proteins and their clients. Cell Mol Life Sci. 2007;64:294–306. - PMC - PubMed
1. Mchaourab HS, Godar JA, Stewart PL. Structure and mechanism of protein stability sensors: Chaperone activity of small heat shock proteins. Biochemistry. 2009;48:3828–3837. - PMC - PubMed
1. Sun Y, MacRae TH. The small heat shock proteins and their role in human disease. FEBS J. 2005;272:2613–2627. - PubMed

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[1] Hartl FU, Hayer-Hartl M. Converging concepts of protein folding in vitro and in vivo. Nat Struct Mol Biol. 2009;16:574–581. - PubMed

[2] Hartl FU, Hayer-Hartl M. Converging concepts of protein folding in vitro and in vivo. Nat Struct Mol Biol. 2009;16:574–581. - PubMed

[3] Saibil HR. Chaperone machines in action. Curr Opin Struct Biol. 2008;18:35–42. - PubMed

[4] Saibil HR. Chaperone machines in action. Curr Opin Struct Biol. 2008;18:35–42. - PubMed

[5] Nakamoto H, Vígh L. The small heat shock proteins and their clients. Cell Mol Life Sci. 2007;64:294–306. - PMC - PubMed

[6] Nakamoto H, Vígh L. The small heat shock proteins and their clients. Cell Mol Life Sci. 2007;64:294–306. - PMC - PubMed

[7] Mchaourab HS, Godar JA, Stewart PL. Structure and mechanism of protein stability sensors: Chaperone activity of small heat shock proteins. Biochemistry. 2009;48:3828–3837. - PMC - PubMed

[8] Mchaourab HS, Godar JA, Stewart PL. Structure and mechanism of protein stability sensors: Chaperone activity of small heat shock proteins. Biochemistry. 2009;48:3828–3837. - PMC - PubMed

[9] Sun Y, MacRae TH. The small heat shock proteins and their role in human disease. FEBS J. 2005;272:2613–2627. - PubMed

[10] Sun Y, MacRae TH. The small heat shock proteins and their role in human disease. FEBS J. 2005;272:2613–2627. - PubMed

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Nature's molecular sponges: small heat shock proteins grow into their chaperone roles

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Nature's molecular sponges: small heat shock proteins grow into their chaperone roles

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