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.
Spiechowicz
Magdalena
M
Nencki Institute of Experimental Biology, 3 Pasteur Street, 02-093 Warsaw, Poland.
Zylicz
Alicja
A
Bieganowski
Paweł
P
Kuznicki
Jacek
J
Filipek
Anna
A
D001665:Binding Sites; D018797:Cell Cycle Proteins / Q000378:metabolism*; D045744:Cell Line, Tumor; D018840:HSP70 Heat-Shock Proteins / Q000378:metabolism*; D006801:Humans; D007822:Laryngeal Neoplasms / Q000378:metabolism*; D011485:Protein Binding / Q000187:drug effects; D000075383:S100 Calcium Binding Protein A6; D009418:S100 Proteins / Q000378:metabolism*; D015398:Signal Transduction / Q000187:drug effects*
D018797:Cell Cycle Proteins; D018840:HSP70 Heat-Shock Proteins; D000075383:S100 Calcium Binding Protein A6; D009418:S100 Proteins; C490164:SUGT1 protein, human; C055351:S100A6 protein, human