Source:http://linkedlifedata.com/resource/pubmed/id/12615054
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2003-3-4
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pubmed:abstractText |
MRP2, a member of the ABC protein superfamily, functions as an ATP-dependent export pump for anionic conjugates in the apical membranes of epithelial cells. It has been reported that the trafficking of MRP2 is modulated by PKC. Adjacent to the C-terminal PDZ binding motif, which may be involved in the targeting of MRP2, we found a potential PKC phosphorylation site (Ser(1542)). Therefore, we examined the interaction of MRP2 and its phosphorylation-mimicking mutants with different PDZ proteins (EBP50, E3KARP, PDZK1, IKEPP, beta2-syntrophin, and SAP-97). The binding of these PDZ proteins to CFTR and ABCA1, other ABC proteins, possessing PDZ binding motif, was also studied. We observed a strong binding of apically localized PDZ proteins to both MRP2 and CFTR, whereas beta2-syntrophin exhibited binding only to ABCA1. The phosphorylation-mimicking MRP2 mutant and a phosphorylated C-terminal MRP2 peptide showed significantly increased binding to IKEPP, EBP50, and both individual PDZ domains of EBP50. Our results suggest that phosphorylation of the MRP2 PDZ binding motif has a profound effect on the PDZ binding of MRP2.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/MRP2 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Mitochondrial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Ribosomal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Serine
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0006-291X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
302
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
454-61
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12615054-Amino Acid Motifs,
pubmed-meshheading:12615054-Animals,
pubmed-meshheading:12615054-Blotting, Western,
pubmed-meshheading:12615054-Dose-Response Relationship, Drug,
pubmed-meshheading:12615054-Humans,
pubmed-meshheading:12615054-Insects,
pubmed-meshheading:12615054-Mitochondrial Proteins,
pubmed-meshheading:12615054-Peptides,
pubmed-meshheading:12615054-Phosphorylation,
pubmed-meshheading:12615054-Plasmids,
pubmed-meshheading:12615054-Protein Binding,
pubmed-meshheading:12615054-Protein Structure, Tertiary,
pubmed-meshheading:12615054-Ribosomal Proteins,
pubmed-meshheading:12615054-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:12615054-Serine
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pubmed:year |
2003
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pubmed:articleTitle |
C-terminal phosphorylation of MRP2 modulates its interaction with PDZ proteins.
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pubmed:affiliation |
Department of Molecular Cell Biology, Membrane Research Group of the Hungarian Academy of Sciences, National Medical Center, Diószegi u. 64, 1113 Budapest, Hungary.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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