Source:http://linkedlifedata.com/resource/pubmed/id/12204117
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
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| pubmed:dateCreated |
2002-9-2
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| pubmed:abstractText |
We have identified a novel dual-specificity phosphatase (DSP), called LDP-2 (low-molecular-mass DSP-2), composed of 220 amino acid residues showing high sequence homology to VHR and LDP-1/TMDP, which belong to a family of DSPs with low molecular masses. The LDP-2 gene is ubiquitously expressed, and LDP-2 is localized in the cytoplasm. The main structural feature of LDP-2 is that the serine-156 residue located in the common active site sequence motif, HCXXGXXRS, for DSP is naturally substituted with an alanine residue. The recombinant LDP-2 protein showed extremely low phosphatase activity towards p-nitrophenyl phosphate (pNPP). Back-mutation of Ala-156 in LDP-2 to a serine (A156S mutation) conferred significant phosphatase activity towards pNPP. However, both LDP-2 and LDP-2 (A156S) exhibited substantial phosphatase activities towards both phospho-seryl/threonyl and -tyrosyl residues of myelin basic protein, with similar specific activities. Ala-156 of LDP-2 might be crucially involved in the recognition of a physiological substrate. We analyzed the effect of VHR and LDP-2 on mitogen-activated protein kinases (MAPKs) in vivo. We first found that VHR inhibits the activation of p38 as well as ERK and JNK, with similar efficiency. Under the conditions used, LDP-2 specifically suppressed JNK activation.
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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
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| pubmed:month |
Sep
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| pubmed:issn |
0021-924X
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
132
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
463-70
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| pubmed:dateRevised |
2007-12-19
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| pubmed:meshHeading |
pubmed-meshheading:12204117-Amino Acid Sequence,
pubmed-meshheading:12204117-Animals,
pubmed-meshheading:12204117-Base Sequence,
pubmed-meshheading:12204117-COS Cells,
pubmed-meshheading:12204117-Cloning, Molecular,
pubmed-meshheading:12204117-DNA, Complementary,
pubmed-meshheading:12204117-HeLa Cells,
pubmed-meshheading:12204117-Humans,
pubmed-meshheading:12204117-Kinetics,
pubmed-meshheading:12204117-Molecular Sequence Data,
pubmed-meshheading:12204117-Molecular Weight,
pubmed-meshheading:12204117-Mutagenesis,
pubmed-meshheading:12204117-Phosphorylation,
pubmed-meshheading:12204117-Protein Phosphatase 2,
pubmed-meshheading:12204117-Protein Tyrosine Phosphatases,
pubmed-meshheading:12204117-Recombinant Proteins,
pubmed-meshheading:12204117-Sequence Homology, Amino Acid,
pubmed-meshheading:12204117-Substrate Specificity
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| pubmed:year |
2002
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| pubmed:articleTitle |
A novel low-molecular-mass dual-specificity phosphatase, LDP-2, with a naturally occurring substitution that affects substrate specificity.
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| pubmed:affiliation |
Division of Biochemical Oncology and Immunology, Institute for Genetic Medicine, Hokkaido University, Kita-ku, Sapporo 060-0815, Japan.
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| pubmed:publicationType |
Journal Article
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