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Androgen receptor RIME using LNCaP cells

ABSTRACT: Rapid immunoprecipitation mass spectrometry of endogenous protein (RIME) was conducted to examine interactome of androgen receptor (AR) in LNCaP cells.

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Atsushi Yokoyama

PROVIDER: PXD024030 | JPOST Repository | Fri Sep 10 00:00:00 BST 2021

REPOSITORIES: jPOST

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Publications

Identification and Functional Characterization of a Novel Androgen Receptor Coregulator, EAP1.

Yokoyama Atsushi A Kouketsu Takumi T Otsubo Yuri Y Noro Erika E Sawatsubashi Shun S Shima Hiroki H Satoh Ikuro I Kawamura Sadafumi S Suzuki Takashi T Igarashi Kazuhiko K Sugawara Akira A

Journal of the Endocrine Society 20210913 11

The androgen receptor (AR) plays an essential role in the development of prostate cancer, and androgen-deprivation therapy is used as a first-line treatment for prostate cancer. However, under androgen-deprivation therapy, castration-resistant prostate cancer inevitably arises, suggesting that the interacting transcriptional coregulators of AR are promising targets for developing novel therapeutics. In this study, we used novel proteomic techniques to evaluate the AR interactome, including bioch ...[more]

PMID: 34585037

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Androgen receptor RIME in prostate cancer cells

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Project description:Androgen Receptor (AR) is a key player in prostate cancer development and progression. Here, we applied immunoprecipitation mass spectrometry of endogenous AR in LNCaP cells to identify individual components of the AR transcription complex. In total, 66 known and novel AR interactors were identified in the presence of R1881, which were critically and selectively required in AR-driven prostate cancer cell proliferation. AR interactors required for LNCaP proliferation were profiled using ChIP-seq, identifying distinct genomic subcomplexes of AR interaction partners. Interestingly, three major subgroups of genomic subcomplexes were identified, where a selective gain-of-function for AR was identified in tumorigenesis, dictated by FOXA1 and HOXB13. Jointly, our study reveals subclasses of the AR transcription complex formation and composition, that is dictated by overexpression of AR-interactors, resulting in reprogramming of the AR cistrome and interactome in a genomic location-specific manner.

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Overexpression of NFIB and YBX1 in MCF-7 cells

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A quantitative mass spectrometry-based approach to monitor the dynamics of endogenous chromatin-associated protein complexes

Project description:Understanding the dynamics of endogenous protein-protein interactions in complex networks is pivotal in deciphering the mechanisms underlying diseases such as cancer. To enable the in-depth analysis of protein interactions in chromatin-associated protein complexes, we have previously developed a method termed RIME (Rapid Immunoprecipitation Mass spectrometry of Endogenous proteins). Here, we present a quantitative multiplexed method (qPLEX-RIME), which integrates RIME with isobaric labelling and tribrid mass spectrometry for the study of protein interactome dynamics in a quantitative fashion with increased sensitivity. Using the qPLEX-RIME method, we delineated the temporal changes of the Estrogen Receptor alpha (ERα) interactome in breast cancer cells treated with 4-hydrotamoxifen and we successfully identified endogenous ERα-associated proteins in human Patient Derived Xenograft (PDX) tumours and in primary human breast cancer clinical tissue. Our results demonstrate that the combination of RIME with isobaric labelling offers a powerful tool for the in-depth and quantitative characterization of protein interactome dynamics which is applicable to clinical samples.

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