RWDD1 interacts with the ligand binding domain of the androgen receptor and acts as a coactivator of androgen-dependent transactivation

Helga Grötsch; Marlene Kunert; Katrin A. Mooslehner; Zhigang Gao; Dagmar Struve; Ieuan A. Hughes; Olaf Hiort; Ralf Werner

doi:10.1016/j.mce.2012.02.020

RWDD1 interacts with the ligand binding domain of the androgen receptor and acts as a coactivator of androgen-dependent transactivation

Helga Grötsch, Marlene Kunert, Katrin A. Mooslehner, Zhigang Gao, Dagmar Struve, Ieuan A. Hughes, Olaf Hiort, Ralf Werner^*

^*Corresponding author for this work

Clinic of Pediatric and Adolescent Medicine

9 Citations (Scopus)

Abstract

During embryogenesis, the development of the male genital is dependent on androgens. Their actions are mediated by the androgen receptor (AR), which functions as a transcription factor. To identify AR coregulators that support AR action during the critical time window of androgen-dependent development in the genital tubercle of male mice, we performed yeast two-hybrid screenings with cDNA libraries of genital tubercles from male mouse embryos using human AR as bait. RWD domain containing 1 (RWDD1) was identified as an AR-interacting protein from three independent libraries of the embryonic days E15, E16 and E17. The interaction between the AR and RWDD1 was confirmed in vitro and in vivo and the ligand binding domain of the AR was shown to be sufficient to mediate the interaction. RWDD1 enhanced AR-dependent transactivation in reporter assays with promoters of different complexity and in different cell lines. These results suggest that RWDD1 functions as a coactivator of androgen-dependent transcription.

Original language	English
Journal	Molecular and Cellular Endocrinology
Volume	358
Issue number	1
Pages (from-to)	53-62
Number of pages	10
ISSN	0303-7207
DOIs	https://doi.org/10.1016/j.mce.2012.02.020
Publication status	Published - 06.07.2012

Funding

The research leading to these results has received funding from the European Community’s Seventh Framework Programme (FP7/2007–2013) under Grant Agreement No. 201444 (EuroDSD). H. Grötsch is a recipient of a Grant from the Medical Faculty of the University of Lübeck, Grant No. E19-2011. We thank H. Merz and A. Dummer from the Department of Pathology of the University of Lübeck for technical support with paraffin-embedding and tissue sample preparation and A.O. Brinkmann, F. Claessens and P.M. Holterhus for providing plasmids. We thank B. Brix for critical reading of the manuscript and M. Szaszak for technical help with the microscope. Microscopy equipment was funded by a Grant from the Medical Faculty of the University of Lübeck, Grant No. E01-2011.

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being
SDG 5 Gender Equality
SDG 10 Reduced Inequalities

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10.1016/j.mce.2012.02.020

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title = "RWDD1 interacts with the ligand binding domain of the androgen receptor and acts as a coactivator of androgen-dependent transactivation",

abstract = "During embryogenesis, the development of the male genital is dependent on androgens. Their actions are mediated by the androgen receptor (AR), which functions as a transcription factor. To identify AR coregulators that support AR action during the critical time window of androgen-dependent development in the genital tubercle of male mice, we performed yeast two-hybrid screenings with cDNA libraries of genital tubercles from male mouse embryos using human AR as bait. RWD domain containing 1 (RWDD1) was identified as an AR-interacting protein from three independent libraries of the embryonic days E15, E16 and E17. The interaction between the AR and RWDD1 was confirmed in vitro and in vivo and the ligand binding domain of the AR was shown to be sufficient to mediate the interaction. RWDD1 enhanced AR-dependent transactivation in reporter assays with promoters of different complexity and in different cell lines. These results suggest that RWDD1 functions as a coactivator of androgen-dependent transcription.",

author = "Helga Gr{\"o}tsch and Marlene Kunert and Mooslehner, \{Katrin A.\} and Zhigang Gao and Dagmar Struve and Hughes, \{Ieuan A.\} and Olaf Hiort and Ralf Werner",

note = "Funding Information: The research leading to these results has received funding from the European Community{\textquoteright}s Seventh Framework Programme (FP7/2007–2013) under Grant Agreement No. 201444 (EuroDSD). H. Gr{\"o}tsch is a recipient of a Grant from the Medical Faculty of the University of L{\"u}beck, Grant No. E19-2011. Funding Information: We thank H. Merz and A. Dummer from the Department of Pathology of the University of L{\"u}beck for technical support with paraffin-embedding and tissue sample preparation and A.O. Brinkmann, F. Claessens and P.M. Holterhus for providing plasmids. We thank B. Brix for critical reading of the manuscript and M. Szaszak for technical help with the microscope. Microscopy equipment was funded by a Grant from the Medical Faculty of the University of L{\"u}beck, Grant No. E01-2011. Copyright: Copyright 2012 Elsevier B.V., All rights reserved.",

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doi = "10.1016/j.mce.2012.02.020",

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AU - Grötsch, Helga

AU - Kunert, Marlene

AU - Mooslehner, Katrin A.

AU - Gao, Zhigang

AU - Struve, Dagmar

AU - Hughes, Ieuan A.

AU - Hiort, Olaf

AU - Werner, Ralf

N1 - Funding Information: The research leading to these results has received funding from the European Community’s Seventh Framework Programme (FP7/2007–2013) under Grant Agreement No. 201444 (EuroDSD). H. Grötsch is a recipient of a Grant from the Medical Faculty of the University of Lübeck, Grant No. E19-2011. Funding Information: We thank H. Merz and A. Dummer from the Department of Pathology of the University of Lübeck for technical support with paraffin-embedding and tissue sample preparation and A.O. Brinkmann, F. Claessens and P.M. Holterhus for providing plasmids. We thank B. Brix for critical reading of the manuscript and M. Szaszak for technical help with the microscope. Microscopy equipment was funded by a Grant from the Medical Faculty of the University of Lübeck, Grant No. E01-2011. Copyright: Copyright 2012 Elsevier B.V., All rights reserved.

PY - 2012/7/6

Y1 - 2012/7/6

N2 - During embryogenesis, the development of the male genital is dependent on androgens. Their actions are mediated by the androgen receptor (AR), which functions as a transcription factor. To identify AR coregulators that support AR action during the critical time window of androgen-dependent development in the genital tubercle of male mice, we performed yeast two-hybrid screenings with cDNA libraries of genital tubercles from male mouse embryos using human AR as bait. RWD domain containing 1 (RWDD1) was identified as an AR-interacting protein from three independent libraries of the embryonic days E15, E16 and E17. The interaction between the AR and RWDD1 was confirmed in vitro and in vivo and the ligand binding domain of the AR was shown to be sufficient to mediate the interaction. RWDD1 enhanced AR-dependent transactivation in reporter assays with promoters of different complexity and in different cell lines. These results suggest that RWDD1 functions as a coactivator of androgen-dependent transcription.

AB - During embryogenesis, the development of the male genital is dependent on androgens. Their actions are mediated by the androgen receptor (AR), which functions as a transcription factor. To identify AR coregulators that support AR action during the critical time window of androgen-dependent development in the genital tubercle of male mice, we performed yeast two-hybrid screenings with cDNA libraries of genital tubercles from male mouse embryos using human AR as bait. RWD domain containing 1 (RWDD1) was identified as an AR-interacting protein from three independent libraries of the embryonic days E15, E16 and E17. The interaction between the AR and RWDD1 was confirmed in vitro and in vivo and the ligand binding domain of the AR was shown to be sufficient to mediate the interaction. RWDD1 enhanced AR-dependent transactivation in reporter assays with promoters of different complexity and in different cell lines. These results suggest that RWDD1 functions as a coactivator of androgen-dependent transcription.

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JO - Molecular and Cellular Endocrinology

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ER -

RWDD1 interacts with the ligand binding domain of the androgen receptor and acts as a coactivator of androgen-dependent transactivation

Abstract

Funding

UN SDGs

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