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Ectopic expression studies of the J‐protein Swa2 and its potential role in yeast prion propagation (567.2)
Author(s) -
Rockman Michael,
Troisi Elizabeth,
Hines Justin
Publication year - 2014
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.28.1_supplement.567.2
Subject(s) - yeast , clathrin , chaperone (clinical) , microbiology and biotechnology , biology , endocytosis , vesicular transport protein , fungal prion , saccharomyces cerevisiae , vesicle , biochemistry , cell , medicine , pathology , membrane
Yeast prions require a core set of chaperone proteins (Sis1, Ssa1, and Hsp104) for stable propagation in yeast, and yet some prions exhibit requirements for additional chaperone activities, indicating that prion‐chaperone requirements are heterogeneous. Preliminary data indicate an additional uncharacterized role for the J‐protein Swa2 in yeast prion biology. Swa2 is the sole yeast homolog of mammalian protein auxilin, which functions in vesicle‐mediated endocytosis by disassembling the structural lattice formed by the protein clathrin. Likewise, Swa2 is required for clathrin‐vesicle uncoating in yeast, presumably by recruiting Hsp70 and stabilizing the Hsp70•clathrin complex. Gene dissection analysis by method of plasmid shuffling and tetracycline repression of Swa2 protein expression are the two primary methods utilized to explore the potential role of Swa2 in yeast prion propagation. Given Swa2’s known role in clathrin uncoating, we expect that mechanisms identified with further research may involve the cellular vesicle trafficking, providing a direct connection between these systems and yeast prion inheritance.