Key result
A novel protein, RILP, was cloned and identified as a putative nuclear translocation receptor required for the nuclear localization of the transcriptional repressor REST/NRSF and REST4.
The discovery of RILP identifies a putative nuclear translocation receptor for the transcriptional repressor REST/NRSF and REST4.
RILP identification extends molecular understanding of REST regulation; leaves open any clinical relevance.
The transcriptional repressor REST/NRSF (RE-1 silencing transcription factor/neuron-restrictive silencer factor) and the transcriptional regulator REST4 share an N-terminal zinc finger domain structure involved in nuclear targeting. Using this domain as bait in a yeast two-hybrid screen, a novel protein that contains three LIM domains, putative nuclear localization sequences, protein kinase A phosphorylation sites, and a CAAX prenylation motif was isolated. This protein, which is localized around the nucleus, is involved in determining the nuclear localization of REST4 and REST/NRSF. We propose the name RILP, for REST/NRSF-interacting LIM domain protein, to label this novel protein. RILP appears to serve as a nuclear receptor for REST/NRSF, REST4, and possibly other transcription factors.
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Shimojo et al. (2003) studied this question. RILP cloning and characterization was evaluated. A novel protein, RILP, was cloned and identified as a putative nuclear translocation receptor required for the nuclear localization of the transcriptional repressor REST/NRSF and REST4.
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