Hsp110 Cooperates with Different Cytosolic HSP70 Systems in a Pathway for de Novo Folding

Yam, Alice; Albanèse, Véronique; Lin, Hen-Tzu Jill; Frydman, Judith

doi:10.1074/jbc.m503615200

Cited by 84 publications

(103 citation statements)

References 48 publications

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“…Sse1 has been implicated in Hsp70-mediated protein folding at the ribosome, Hsp90 chaperoning of signal transduction, and post-translational translocation of pre-pro ␣-factor (21,22,37,38). Both Sse1 and Fes1 participate in Hsp70-dependent ubiquitination and degradation of misfolded proteins (39 -43).…”

mentioning

confidence: 99%

Hierarchical Functional Specificity of Cytosolic Heat Shock Protein 70 (Hsp70) Nucleotide Exchange Factors in Yeast

Abrams¹,

Verghese²,

Gibney³

et al. 2014

Journal of Biological Chemistry

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mentioning

confidence: 99%

Hierarchical Functional Specificity of Cytosolic Heat Shock Protein 70 (Hsp70) Nucleotide Exchange Factors in Yeast

Abrams¹,

Verghese²,

Gibney³

et al. 2014

Journal of Biological Chemistry

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“…A special feature of Saccharomyces cerevisiae is that it has two Hsp70's dedicated to aiding the folding of newly synthesized proteins. These are Ssb1 and Ssb2, the chaperones responsible for the bulk of Hsp70 binding to ribosomebound nascent chains Craig et al 2003;Yam et al 2005). The peptide-binding activity of Ssb is dependent on the ribosome-associated complex (RAC) of an Hsp40 protein, Zuo1, and of another Hsp70 protein, Ssz1 (Yan et al 1998;Michimoto et al 2000;Gautschi et al 2001;Huang et al 2005).…”

mentioning

confidence: 99%

Why Molecular Chaperones Buffer Mutational Damage: A Case Study With a Yeast Hsp40/70 System

et al. 2006

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The malfunctioning of molecular chaperones may result in uncovering genetic variation. The molecular basis of this phenomenon remains largely unknown. Chaperones rescue proteins unfolded by environmental stresses and therefore they might also help to stabilize mutated proteins and thus mask damages. To test this hypothesis, we carried out a genomewide mutagenesis followed by a screen for mutations that were synthetically harmful when the RAC-Ssb1/2 cytosolic chaperones were inactive. Mutants with such a phenotype were found and mapped to single nucleotide substitutions. However, neither the genes identified nor the nature of genetic lesions implied that folding of the mutated proteins was being supported by the chaperones. In a second screen, we identified temperature-sensitive (ts) mutants, a phenotype indicative of structural instability of proteins. We tested these for an association with sensitivity to loss of chaperone activity but found no such correlation as might have been expected if the chaperones assisted the folding of mutant proteins. Thus, molecular chaperones can mask the negative effects of mutations but the mechanism of such buffering need not be direct. A plausible role of chaperones is to stabilize genetic networks, thus making them more tolerant to malfunctioning of their constituents.

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“…Consistent with this, both Hsp70 and Hsp105 have been implicated in co-translational folding of membrane proteins in the ER (10,51). CFTR quality control in the ER can occur coincident with translation through RMA1 (52)(53)(54).…”

Section: Discussionmentioning

confidence: 63%

“…Hsp105 facilitates the nucleotide exchange of Hsc70 (8,9). In Yeast, Hsp105 homologue Sse1 collaborates with Hsp70 homologue Ssb or Ssa in regulating the co-translational or post-translational folding of cellular proteins, respectively (10). Sse1 is specifically required for Ssa1-mediated post-translational translocation of the yeast mating pheromone ␣-factor into the endoplasmic reticulum (ER) (6).…”

mentioning

confidence: 99%

Human Heat Shock Protein 105/110 kDa (Hsp105/110) Regulates Biogenesis and Quality Control of Misfolded Cystic Fibrosis Transmembrane Conductance Regulator at Multiple Levels

Saxena

Banasavadi-Siddegowda

Fan

et al. 2012

Journal of Biological Chemistry

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Background: Hsp105 prevents protein aggregation, accelerates Hsc70 nucleotide exchange, and functionally relates to Hsp90. Results: Hsp105 facilitates CFTR quality control coincident with translation, enhances its post-translational folding, and stabilizes misfolded CFTR at cell periphery. Conclusion: Hsp105 is a versatile regulator in CFTR folding and quality control. Significance: Hsp105 plays distinct roles in CFTR folding from other Hsc70 nucleotide exchange factors.

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Hsp110 Cooperates with Different Cytosolic HSP70 Systems in a Pathway for de Novo Folding

Cited by 84 publications

References 48 publications

Hierarchical Functional Specificity of Cytosolic Heat Shock Protein 70 (Hsp70) Nucleotide Exchange Factors in Yeast

Hierarchical Functional Specificity of Cytosolic Heat Shock Protein 70 (Hsp70) Nucleotide Exchange Factors in Yeast

Why Molecular Chaperones Buffer Mutational Damage: A Case Study With a Yeast Hsp40/70 System

Human Heat Shock Protein 105/110 kDa (Hsp105/110) Regulates Biogenesis and Quality Control of Misfolded Cystic Fibrosis Transmembrane Conductance Regulator at Multiple Levels

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