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Destruction of Full-Length Androgen Receptor by Wild-Type SPOP, but Not Prostate-Cancer-Associated Mutants

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An, Jian, Wang, Chenji, Deng, Yibin, Yu, Long, Huang, Haojie·2014·Cell Reports

DOI 10.1016/j.celrep.2014.01.013

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Abstract

The SPOP E3 ubiquitin ligase gene is frequently mutated in human prostate cancers. Here, we demonstrate that SPOP recognizes a Ser/Thr-rich degron in the hinge domain of androgen receptor (AR) and induces degradation of full-length AR and inhibition of AR-mediated gene transcription and prostate cancer cell growth. AR splicing variants, most of which lack the hinge domain, escape SPOP-mediated degradation. Prostate-cancer-associated mutants of SPOP cannot bind to and promote AR destruction. Furthermore, androgens antagonize SPOP-mediated degradation of AR, whereas antiandrogens promote this process. This study identifies AR as a bona fide substrate of SPOP and elucidates a role of SPOP mutations in prostate cancer, thus implying the importance of this pathway in resistance to antiandrogen therapy of prostate cancer.

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See all 260

Authors: An, J., Wang, C., Deng, Y., Yu, L., & Huang, H.
Venue: Cell Reports
Publisher: Elsevier BV
Published: 2014-02
Volume: 6
Issue: 4
Pages: 657-669
ISSN: 2211-1247 (ISSN-L)
DOI: 10.1016/j.celrep.2014.01.013
OpenAlex: W2042756500
Cited by: 260
References: 46
FWCI: 17.20
Type: journal article
Language: en
Open access: gold

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Destruction of Full-Length Androgen Receptor by Wild-Type SPOP, but Not Prostate-Cancer-Associated Mutants

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