SGT, a Hsp90beta binding partner, is accumulated in the nucleus during cell apoptosis.
In this study, we reported that small glutamine-rich TPR-containing protein (SGT) interacted with not only Hsp90alpha but also Hsp90beta. Confocal analysis showed that treatment of cells with Hsp90-specific inhibitor geldanamycin (GA) disrupted the interaction of SGT with Hsp90beta and this contributed to the increase of nuclear localization of SGT in HeLa cells. The increased nuclear localization of SGT was further confirmed by the Western blotting in GA-treated HeLa cells and H1299 cells. In our previous study, SGT was found to be a new pro-apoptotic factor, so we wondered whether the sub-cellular localization of SGT was related with cell apoptosis. By confocal analysis we found that the nuclear import of SGT was significantly increased in STS-induced apoptotic HeLa cells, which implied that the sub-cellular localization of SGT was closely associated with Hsp90beta and apoptosis.
Key Laboratory of Medical Molecular Virology Ministry of Education and Health, Gene Research Center, Shanghai Medical College and Institutes of Biomedical Sciences of Fudan University, Shanghai 200032, PR China.
Hongyan
H
Yin
Hanzhou
H
Wang
Hongliang
H
Zong
Xiaoning
X
Chen
Yanlin
Y
Wang
Xiaojing
X
Yun
Yihong
Y
Wu
Jiadong
J
Wang
Jianxin
J
Gu
D021581:Active Transport, Cell Nucleus; D017209:Apoptosis; D002352:Carrier Proteins / Q000096:biosynthesis / Q000378:metabolism*; D002460:Cell Line; D002467:Cell Nucleus / Q000378:metabolism*; D003593:Cytoplasm / Q000378:metabolism; D018841:HSP90 Heat-Shock Proteins / Q000037:antagonists & inhibitors / Q000378:metabolism*; D006801:Humans; D018832:Molecular Chaperones; D011485:Protein Binding
D002352:Carrier Proteins; D018841:HSP90 Heat-Shock Proteins; C493165:HSP90AB1 protein, human; D018832:Molecular Chaperones; C114575:SGTA protein, human