SIS1 Antibody

1. Differences in sensitivity of prion fragmentation to Sis1 and in relative inputs of fragmentation and malpartition in prion propagation result in opposite effects of Sis1 relocalization on [PSI (+)] and [URE3]. PMID: 28932898
2. Sis1 plays a role in prion replication. PMID: 25329162
3. Interaction of Sis1 with EEVD(Hsp70) minimizes transfer of Sis1-bound clients to Hsp70s that are primed for client transfer to folding and translocation pathways by their preassociation with EEVD binding adaptor proteins. PMID: 25687964
4. This conservation of function is also prion-variant dependent, indicating that only one of the two Sis1-prion functions may have been maintained in eukaryotic chaperone evolution. PMID: 25058638
5. The stability of Sis1 and mutants that had the central domains (named Gly/Met rich domain and C-terminal Domain I) deleted or switched to those of Ydj1 were evaluated to gain insight into the role of these regions in the structure and function of Sis1. PMID: 23227221
6. Sis1 is a yeast member of the Type II Hsp40s family and in a highly conserved alpha-helical N-terminal J-domain, a disordered middle region (divided into glycine/phenylalanine (G/F) and glycine/methionine (G/M) rich regions) and two C-terminal sub-domains. PMID: 22011374
7. Functions of yeast Hsp40 chaperone Sis1p are dispensable for prion propagation but important for prion curing and protection from prion toxicity. PMID: 21555396
8. Genetic experiments showed that Sis1 is an essential protein and apparently plays a functional role at assembly or disassembly of protein complexes. PMID: 17985367
9. In vivo monitoring of the prion replication cycle reveals a critical role for Sis1 in delivering substrates to Hsp104. PMID: 19026788

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KEGG: sce:YNL007C

STRING: 4932.YNL007C