Both mammalian cells and yeast cells possess a chaperone network composed of Hsp70, Hsp90, Hop/Sti1, Hsp40 and p23/Sba1. During the multichaperone cycle, substrate proteins of Hsp90 must be transferred from Hsp70 to Hsp90 in order to mature and aquire their active form. Formation of a complex between Hsp70 and Hsp90 is facilitated by the adaptor protein Hop/Sti1. In the frame of this work, the adaptor protein Hop/Sti1 was characterized and important functional parts of the protein could be elucidated. in vivo assays in both the yeast S. cerevisiae and human HeLa cells revealed relevant segments of Hop/Sti1 for the activation of the human glucocorticoid receptor and v-Src kinase. Based on the aquired data, a new model is proposed for the function of Hop/Sti1 domains.
«Both mammalian cells and yeast cells possess a chaperone network composed of Hsp70, Hsp90, Hop/Sti1, Hsp40 and p23/Sba1. During the multichaperone cycle, substrate proteins of Hsp90 must be transferred from Hsp70 to Hsp90 in order to mature and aquire their active form. Formation of a complex between Hsp70 and Hsp90 is facilitated by the adaptor protein Hop/Sti1. In the frame of this work, the adaptor protein Hop/Sti1 was characterized and important functional parts of the protein could be eluci...
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