Fig. 5 | Nature Communications

Fig. 5

From: Phosphorylation induced cochaperone unfolding promotes kinase recruitment and client class-specific Hsp90 phosphorylation

Fig. 5

Phosphorylation of Hsp90 in the context of in vitro-assembled complexes. Mass spectrometry intensity ratios of Yes-modified Hsp90α peptides over the corresponding unmodified peptides for positions Y61, Y160, Y197, Y438, Y492, and Y604. Ratios are normalized to the highest-detected phosphorylation levels among five different liganded states of Hsp90α: free, in a binary complex with wild-type Cdc37 (C), or in a ternary complex with bRaf and Cdc37 variants (wild type = C-K, doubly non-phosphorylatable = CFF-K, singly non-phosphorylatable = CF-K, and double phosphomimetic = CEE-K). Error bars are defined as s.d., over two replicates

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