SSE1 Antibody

1. The Sse1/Hsp70 complex maintains the solubility of FLAG-Pgk1-300, thereby stimulating its Upf-dependent degradation by the proteasomes. PMID: 28483531
2. 13 novel mutations in Sse1 have varying effects on both the ability of S. cerevisiae to propagate the [PSI+] prion and also to grow at increased temperatures. PMID: 23797105
3. The role of Hsp110 Sse1 as a nucleotide exchange factor for the Hsp70 chaperones Ssa1/Ssa2 is required for maintaining proper distribution of kinesin-5 motors within the spindle, which is subsequently required for bipolar spindle assembly in S phase. PMID: 22908312
4. Findings support a model in which Hsp110 chaperones control the fate of some client proteins by influencing the decision to fold or degrade as dictated by the Hsp70-Hsp90 chaperone environment. PMID: 20237159
5. The molecular chaperone Sse1 and the growth control protein kinase Sch9 collaborate to regulate protein kinase A signaling. PMID: 15879503
6. Data suggest that Sse1(ATP) may be an evolutionary vestige of the Hsp70(ATP) state, and an analysis of 64 mutant variants in Sse1 and three Hsp70 homologs supports this hypothesis. PMID: 17923091
7. NEF activity of Sse1 requires nucleotide binding and let us propose a new model for Hsp110 function. PMID: 18218635
8. mechanistic model wherein Sse1 functionally partners with Hsp90 as an Hsp70 nucleotide exchange factor to promote client protein maturation and interaction with downstream effectors PMID: 18478233
9. The structure of an Hsp110:Hsc70 nucleotide exchange complex, is reported. PMID: 18550409
10. Data suggest that Sse1p does not employ the nucleotide-dependent allostery and peptide-binding mode of canonical Hsp70s, and that direct interactions of substrate with Sse1p may support Hsp70-assisted protein folding in a cooperative process. PMID: 18555782

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KEGG: sce:YPL106C

STRING: 4932.YPL106C