期刊
MOLECULAR AND CELLULAR BIOLOGY
卷 26, 期 5, 页码 1722-1730出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/MCB.26.5.1722-1730.2006
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资金
- NCI NIH HHS [R01 CA026869, R01 CA26869] Funding Source: Medline
- NIDDK NIH HHS [R01 DK059284, R01 DK 59284] Funding Source: Medline
The hsp90 chaperoning pathway is a multiprotein system that is required for the production or activation of many cell regulatory proteins, including the progesterone receptor (PR). We report here the identity of GCUNC-45 as a novel modulator of PR chaperoning by hsp90. GCUNC-45, previously implicated in the activities of myosins, can interact in vivo and in vitro with both PR-A and PR-B and with hsp90. Overexpression and knockdown experiments show GCUNC-45 to be a positive factor in promoting PR function in the cell. GCUNC-45 binds to the ATP-binding domain of hsp90 to prevent the activation of its ATPase activity by the cochaperone Aha1. This effect limits PR chaperoning by hsp90, but this can be reversed by FKBP52, a cochaperone that is thought to act later in the pathway. These findings reveal a new cochaperone binding site near the N terminus of hsp90, add insight on the role of FKBP52, and identify GCUNC-45 as a novel regulator of the PR signaling pathway.
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