Hsp70 is a new target of Sgt1--an interaction modulated by S100A6.

In this work, we identified Hsp70 as a novel target of the Sgt1 protein. Using co-immunoprecipitation, affinity chromatography and ELISA we showed that, besides Hsp90, Sgt1 interacts with the heat shock protein, Hsp70. We also found that a deletion mutant of Sgt1, devoid of the C-terminal region, did not bind ...
to either Hsp70 or Hsp90 proteins. Overexpression of S100A6, a calcium binding protein that interacts with the C-terminal part of Sgt1, decreased the amount of chaperone bound to Sgt1. However, the effect of S100A6 on this interaction was not observed in BAPTA/AM treated cells in which Ca(2+) level was decreased. This suggests that the interaction of Sgt1 with Hsp70 and Hsp90 is regulated by S100A6 in a Ca(2+)-dependent manner.
Mesh Terms:
Binding Sites, Cell Cycle Proteins, Cell Line, Tumor, HSP70 Heat-Shock Proteins, Humans, Laryngeal Neoplasms, Protein Binding, S100 Proteins, Signal Transduction
Biochem. Biophys. Res. Commun.
Date: Jun. 15, 2007
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