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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
19
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pubmed:dateCreated |
2010-10-25
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pubmed:abstractText |
With the aim of discovering new molecular interactions of the tight junction protein ZO-2, a two-hybrid screen was performed on a human kidney cDNA library using as bait the middle segment of ZO-2. Through this assay we identified a 24-kDa novel protein herein named ZASP for ZO-2 associated speckle protein. ZO-2/ZASP interaction further confirmed by pull down and immunoprecipitation experiments, requires the presence of the intact PDZ binding motif SQV of ZASP and the third PDZ domain of ZO-2. ZASP mRNA and protein are present in the kidney and in several epithelial cell lines. Endogenous ZASP is expressed primarily in nuclear speckles in co-localization with splicing factor SC-35. Nocodazole treatment and wash out reveals that ZASP disappears from the nucleus during mitosis in accordance with speckle disassembly during metaphase. ZASP amino acid sequence exhibits a canonical nuclear exportation signal and in agreement the protein exits the nucleus through a process mediated by exportin/CRM1. ZASP over-expression blocks the inhibitory activity of ZO-2 on cyclin D1 gene transcription and protein expression. The identification of ZASP helps to unfold the complex nuclear molecular arrays that form on ZO-2 scaffolds.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD1,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin D1,
http://linkedlifedata.com/resource/pubmed/chemical/Karyopherins,
http://linkedlifedata.com/resource/pubmed/chemical/LDB3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/LIM Domain Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/zonula occludens-2 protein
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
1090-2422
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pubmed:author |
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pubmed:copyrightInfo |
Copyright © 2010 Elsevier Inc. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:day |
15
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pubmed:volume |
316
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3124-39
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:20868680-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:20868680-Amino Acid Motifs,
pubmed-meshheading:20868680-Amino Acid Sequence,
pubmed-meshheading:20868680-Animals,
pubmed-meshheading:20868680-Antigens, CD1,
pubmed-meshheading:20868680-Base Sequence,
pubmed-meshheading:20868680-Cell Cycle,
pubmed-meshheading:20868680-Cell Line,
pubmed-meshheading:20868680-Cell Nucleus,
pubmed-meshheading:20868680-Cloning, Molecular,
pubmed-meshheading:20868680-Cyclin D1,
pubmed-meshheading:20868680-Dogs,
pubmed-meshheading:20868680-Gene Expression Regulation,
pubmed-meshheading:20868680-Humans,
pubmed-meshheading:20868680-Immunoprecipitation,
pubmed-meshheading:20868680-Karyopherins,
pubmed-meshheading:20868680-Kidney,
pubmed-meshheading:20868680-LIM Domain Proteins,
pubmed-meshheading:20868680-Membrane Proteins,
pubmed-meshheading:20868680-Molecular Sequence Data,
pubmed-meshheading:20868680-Promoter Regions, Genetic,
pubmed-meshheading:20868680-Protein Binding,
pubmed-meshheading:20868680-Protein Structure, Tertiary,
pubmed-meshheading:20868680-Protein Transport,
pubmed-meshheading:20868680-RNA, Messenger
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pubmed:year |
2010
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pubmed:articleTitle |
Identification of ZASP, a novel protein associated to Zona occludens-2.
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pubmed:affiliation |
Department of Physiology, Biophysics and Neuroscience, Center for Research and Advanced Studies (Cinvestav), México, DF 07360, Mexico.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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