Abstract
Internalization of activated receptors regulates signaling, and endocytic adaptor proteins are well-characterized in clathrin-mediated uptake. One of these adaptor proteins, huntingtin interacting protein 1 (HIP1), induces cellular transformation and is overexpressed in some prostate cancers. We have discovered that HIP1 associates with the androgen receptor through a central coiled coil domain and is recruited to DNA response elements upon androgen stimulation. HIP1 is a novel androgen receptor regulator, I significantly repressing transcription when knocked down using a silencing RNA approach and activating transcription when overexpressed. We have also identified a functional nuclear localization signal at the COOH terminus of HIP1, which contributes to the nuclear translocation of the protein. In conclusion, we have discovered that HIP1 is a nucleocytoplasmic protein capable of associating with membranes and DNA response elements and regulating transcription.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 191-200 |
| Number of pages | 10 |
| Journal | Journal of Cell Biology |
| Volume | 170 |
| Issue number | 2 |
| DOIs | |
| State | Published - Jul 2005 |
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ASJC Scopus subject areas
- Cell Biology
Cite this
Huntingtin interacting protein 1 modulates the transcriptional activity of nuclear hormone receptors. / Mills, Ian G.; Gaughan, Luke; Robson, Craig; Ross, Theodora; McCracken, Stuart; Kelly, John; Neal, David E.
In: Journal of Cell Biology, Vol. 170, No. 2, 07.2005, p. 191-200.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Huntingtin interacting protein 1 modulates the transcriptional activity of nuclear hormone receptors
AU - Mills, Ian G.
AU - Gaughan, Luke
AU - Robson, Craig
AU - Ross, Theodora
AU - McCracken, Stuart
AU - Kelly, John
AU - Neal, David E.
PY - 2005/7
Y1 - 2005/7
N2 - Internalization of activated receptors regulates signaling, and endocytic adaptor proteins are well-characterized in clathrin-mediated uptake. One of these adaptor proteins, huntingtin interacting protein 1 (HIP1), induces cellular transformation and is overexpressed in some prostate cancers. We have discovered that HIP1 associates with the androgen receptor through a central coiled coil domain and is recruited to DNA response elements upon androgen stimulation. HIP1 is a novel androgen receptor regulator, I significantly repressing transcription when knocked down using a silencing RNA approach and activating transcription when overexpressed. We have also identified a functional nuclear localization signal at the COOH terminus of HIP1, which contributes to the nuclear translocation of the protein. In conclusion, we have discovered that HIP1 is a nucleocytoplasmic protein capable of associating with membranes and DNA response elements and regulating transcription.
AB - Internalization of activated receptors regulates signaling, and endocytic adaptor proteins are well-characterized in clathrin-mediated uptake. One of these adaptor proteins, huntingtin interacting protein 1 (HIP1), induces cellular transformation and is overexpressed in some prostate cancers. We have discovered that HIP1 associates with the androgen receptor through a central coiled coil domain and is recruited to DNA response elements upon androgen stimulation. HIP1 is a novel androgen receptor regulator, I significantly repressing transcription when knocked down using a silencing RNA approach and activating transcription when overexpressed. We have also identified a functional nuclear localization signal at the COOH terminus of HIP1, which contributes to the nuclear translocation of the protein. In conclusion, we have discovered that HIP1 is a nucleocytoplasmic protein capable of associating with membranes and DNA response elements and regulating transcription.
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U2 - 10.1083/jcb.200503106
DO - 10.1083/jcb.200503106
M3 - Article
VL - 170
SP - 191
EP - 200
JO - Journal of Cell Biology
JF - Journal of Cell Biology
SN - 0021-9525
IS - 2
ER -