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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
5
|
| pubmed:dateCreated |
1999-3-3
|
| pubmed:databankReference | |
| pubmed:abstractText |
Using a cytoplasmic domain of the peripheral benzodiazepine receptor (PBR) as a bait in the yeast two-hybrid system, we have isolated a cDNA encoding a new protein that specifically interacts with PBR. We named it PRAX-1, for peripheral benzodiazepine receptor-associated protein 1. PRAX-1 is a 1857-amino acid protein, the sequence of which was structurally unrelated to any known proteins. The gene encoding PRAX-1 is located in the q22-q23 region of the long arm of the human chromosome 17. The PRAX-1 mRNA is 7.5 kilobase pairs, predominantly expressed in the central nervous system, pituitary gland, and thymus. At the protein level, we found the PRAX-1 as a single 220-250-kDa protein in the brain and in many different human cell lines tested using specific antibody raised against PRAX-1. Parallel analysis of the PRAX-1 mRNA and protein expression performed in mouse and rat gave similar results. Immunocytochemistry analysis carried out to define the distribution of the PRAX-1 protein in the rat brain showed that PRAX-1 was prevalent in the mesolimbic system, specially abundant in the CA1 subfield of the hippocampus. Exhibiting several domains involved in protein-protein interaction (three proline-rich domains, three leucine-zipper motifs, and an Src homology region 3-like domain), the PRAX-1 may be looked upon as a new adaptator protein. We show that both the Src homology region 3-like domain and a proline-rich domain in PRAX-1 are required for the interaction with PBR. PRAX-1 is a cytoplasmic protein that also partially colocalizes with PBR in the mitochondria, as determined by confocal microscopy and Western blotting. Altogether our observations support a model of interaction implicating PBR and this newly described protein, PRAX-1. As being the first cytoplasmic protein associated with PBR, PRAX-1 is a new tool that opens new fields for exploring PBR biological roles.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jan
|
| pubmed:issn |
0021-9258
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
29
|
| pubmed:volume |
274
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
2938-52
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| pubmed:dateRevised |
2004-11-17
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| pubmed:meshHeading |
pubmed-meshheading:9915832-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:9915832-Amino Acid Sequence,
pubmed-meshheading:9915832-Animals,
pubmed-meshheading:9915832-Base Sequence,
pubmed-meshheading:9915832-Blotting, Western,
pubmed-meshheading:9915832-Brain,
pubmed-meshheading:9915832-Carrier Proteins,
pubmed-meshheading:9915832-Chickens,
pubmed-meshheading:9915832-Chromosome Banding,
pubmed-meshheading:9915832-Chromosomes, Human, Pair 17,
pubmed-meshheading:9915832-Cloning, Molecular,
pubmed-meshheading:9915832-Consensus Sequence,
pubmed-meshheading:9915832-Humans,
pubmed-meshheading:9915832-In Situ Hybridization, Fluorescence,
pubmed-meshheading:9915832-Mice,
pubmed-meshheading:9915832-Molecular Sequence Data,
pubmed-meshheading:9915832-RNA, Messenger,
pubmed-meshheading:9915832-Rats,
pubmed-meshheading:9915832-Receptors, GABA-A
|
| pubmed:year |
1999
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| pubmed:articleTitle |
Cloning and characterization of PRAX-1. A new protein that specifically interacts with the peripheral benzodiazepine receptor.
|
| pubmed:affiliation |
Immunology Department, Sanofi, 371 rue du Professeur Joseph Blayac, 34184 Montpellier cedex 04, 75013, Paris, France.
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| pubmed:publicationType |
Journal Article
|