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FKBP52 and FKBP51 differentially regulate the stability of estrogen receptor in breast cancer

by Hanaki, Shunsuke , Morimoto, Masahiro , Imai, Hiroyuki , Sato, Yuki , Sakurai, Masashi , Toyama, Tatsuya , Shimada, Midori , Goshima, Takahiro , Shimizu, Hideyuki , Habara, Makoto , Katayama, Yuta , Masaki, Takahiro , Nishikawa, Sayaka

in Biological Sciences / Breast cancer / Breast Neoplasms - metabolism / Cell Biology / Cell growth / Cell Line, Tumor / Cell proliferation / Depletion / Endocrine therapy / Estrogen Receptor alpha - genetics / Estrogen Receptor alpha - metabolism / Estrogen receptors / Estrogens / Female / Fulvestrant / Gene Expression Regulation, Neoplastic / Humans / MCF-7 Cells / Molecular modelling / Protein Stability / Receptors / Regulatory mechanisms (biology) / Stability / Tacrolimus / Tacrolimus Binding Proteins - metabolism / Tacrolimus-binding protein / Tumor cell lines

2022

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FKBP52 and FKBP51 differentially regulate the stability of estrogen receptor in breast cancer

2022

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FKBP52 and FKBP51 differentially regulate the stability of estrogen receptor in breast cancer

2022

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Journal Article

FKBP52 and FKBP51 differentially regulate the stability of estrogen receptor in breast cancer

Hanaki, Shunsuke,

Morimoto, Masahiro,

Imai, Hiroyuki,

Sato, Yuki,

Sakurai, Masashi,

Toyama, Tatsuya,

Shimada, Midori,

Goshima, Takahiro,

Shimizu, Hideyuki,

Habara, Makoto,

Katayama, Yuta,

Masaki, Takahiro,

Nishikawa, Sayaka

2022

Overview

Estrogen receptor α (ERα) is a transcription factor that induces cell proliferation and exhibits increased expression in a large subset of breast cancers. The molecular mechanisms underlying the up-regulation of ERα activity, however, remain poorly understood. We identified FK506-binding protein 52 (FKBP52) as a factor associated with poor prognosis of individuals with ERα-positive breast cancer. We found that FKBP52 interacts with breast cancer susceptibility gene 1 and stabilizes ERα, and is essential for breast cancer cell proliferation. FKBP52 depletion resulted in decreased ERα expression and proliferation in breast cancer cell lines, including MCF7-derived fulvestrant resistance (MFR) cells, suggesting that inhibiting FKBP52 may provide a therapeutic effect for endocrine therapy–resistant breast cancer. In contrast, FKBP51, a closely related molecule to FKBP52, reduced the stability of ERα. Consistent with these findings, FKBP51 was more abundantly expressed in normal tissues than in cancer cells, suggesting that these FKBPs may function in the opposite direction. Collectively, our study shows that FKBP52 and FKBP51 regulate ERα stability in a reciprocal manner and reveals a regulatory mechanism by which the expression of ERα is controlled.

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Publisher

National Academy of Sciences

Subject

Biological Sciences

/ Breast cancer

/ Breast Neoplasms - metabolism