Abstract
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.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Active Transport, Cell Nucleus
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Animals
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Base Sequence
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DNA, Complementary / genetics
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HeLa Cells
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Humans
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In Vitro Techniques
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Mice
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Molecular Sequence Data
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Protein Structure, Tertiary
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RNA Interference
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RNA, Messenger / genetics
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RNA, Messenger / metabolism
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Rats
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Receptors, Cytoplasmic and Nuclear / chemistry
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Receptors, Cytoplasmic and Nuclear / genetics
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Receptors, Cytoplasmic and Nuclear / metabolism*
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Repressor Proteins / chemistry
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Repressor Proteins / genetics
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Repressor Proteins / metabolism*
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Tissue Distribution
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Transcription Factors / chemistry
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Transcription Factors / genetics
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Transcription Factors / metabolism*
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Two-Hybrid System Techniques
Substances
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DNA, Complementary
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RE1-silencing transcription factor
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RNA, Messenger
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Receptors, Cytoplasmic and Nuclear
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Repressor Proteins
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Transcription Factors
Associated data
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GENBANK/AF399843
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GENBANK/AF399844