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Huntingtin interacting protein 1 modulates the transcriptional activity of nuclear hormone receptors.


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, 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.

SUBMITTER: Mills IG 

PROVIDER: S-EPMC2171420 | biostudies-literature | 2005 Jul

REPOSITORIES: biostudies-literature

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Huntingtin interacting protein 1 modulates the transcriptional activity of nuclear hormone receptors.

Mills Ian G IG   Gaughan Luke L   Robson Craig C   Ross Theodora T   McCracken Stuart S   Kelly John J   Neal David E DE  

The Journal of cell biology 20050701 2


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  ...[more]

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