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Cited by 372

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Activation Function 2 in the Human Androgen Receptor Ligand Binding Domain Mediates Interdomain Communication with the NH2-terminal Domain

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He, Bin, Kemppainen, Jon A., Voegel, Johannes J., Gronemeyer, Hinrich, Wilson, Elizabeth M.·1999·Journal of Biological Chemistry
DOI 10.1074/jbc.274.52.37219
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Abstract

Activation function 2 in the ligand binding domain of nuclear receptors forms a hydrophobic cleft that binds the LXXLL motif of p160 transcriptional coactivators. Here we provide evidence that activation function 2 in the androgen receptor serves as the contact site for the androgen dependent NH(2)- and carboxyl-terminal interaction of the androgen receptor and only weakly interacts with p160 coactivators in an LXXLL-dependent manner. Mutagenesis studies indicate that it is the NH(2)-/carboxyl-terminal interaction that is required by activation function 2 to stabilize helix 12 and slow androgen dissociation critical for androgen receptor activity in vivo. The androgen receptor recruits p160 coactivators through its NH(2)-terminal and DNA binding domains in an LXXLL motif-independent manner. The results suggest a novel function for activation function 2 and a unique mechanism of nuclear receptor transactivation.

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Cited by

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Metadata

Authors
He, B., Kemppainen, J. A., Voegel, J. J., Gronemeyer, H., & Wilson, E. M.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1999-12
Volume
274
Issue
52
Pages
37219-37225
ISSN
0021-9258 (ISSN-L)
DOI
10.1074/jbc.274.52.37219
OpenAlex
W2007589116
Cited by
372
References
2
FWCI
11.99
Type
journal article
Language
en
Open access
hybrid
Licence

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CoChat. (2026). Citation check: Activation Function 2 in the Human Androgen Receptor Ligand Binding Domain Mediates Interdomain Communication with the NH2-terminal Domain. https://app.cochat.ai/papers/10.1074/jbc.274.52.37219
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He, B., Kemppainen, J. A., Voegel, J. J., Gronemeyer, H., & Wilson, E. M. (1999). Activation Function 2 in the Human Androgen Receptor Ligand Binding Domain Mediates Interdomain Communication with the NH2-terminal Domain. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.274.52.37219

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