|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
Pt. 3
|
|
pubmed:dateCreated |
2004-10-25
|
|
pubmed:databankReference |
|
|
pubmed:abstractText |
We have isolated a mouse cDNA for a novel dual-specificity phosphatase designated LDP-3 (low-molecular-mass dual-specificity phosphatase 3). The 450 bp open reading frame encodes a protein of 150 amino acids with a predicted molecular mass of 16 kDa. Northern blot and reverse transcription-PCR analyses show that LDP-3 transcripts are expressed in almost all mouse tissues examined. In vitro analyses using several substrates and inhibitors indicate that LDP-3 possesses intrinsic dual-specificity phosphatase activity. When expressed in mammalian cells, LDP-3 protein is localized mainly to the apical submembrane area. Forced expression of LDP-3 does not alter activation of ERK (extracellular-signal-regulated kinase), but rather enhances activation of JNK (c-Jun N-terminal kinase) and p38 and their respective upstream kinases MKK4 (mitogen-activated protein kinase kinase 4) and MKK6 in cells treated with 0.4 M sorbitol. By screening with a variety of stimuli, we found that LDP-3 specifically enhances the osmotic stress-induced activation of JNK and p38.
|
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/15281913-10224087,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15281913-10391943,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15281913-10585869,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15281913-11085983,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15281913-11248552,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15281913-11294822,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15281913-11346645,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15281913-11489891,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15281913-11694501,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15281913-11717427,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15281913-11733513,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15281913-11959861,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15281913-11959862,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15281913-12138158,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15281913-12176346,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15281913-12204117,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15281913-12479873,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15281913-12591617,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15281913-12794087,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15281913-1281213,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15281913-1281549,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15281913-12947390,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15281913-14634666,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15281913-2440339,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15281913-8626452,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15281913-8887669,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15281913-9305639,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15281913-9535927,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15281913-9558074,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15281913-9566916
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Nov
|
|
pubmed:issn |
1470-8728
|
|
pubmed:author |
|
|
pubmed:issnType |
Electronic
|
|
pubmed:day |
1
|
|
pubmed:volume |
383
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
447-55
|
|
pubmed:dateRevised |
2009-11-19
|
|
pubmed:meshHeading |
pubmed-meshheading:15281913-Amino Acid Sequence,
pubmed-meshheading:15281913-Animals,
pubmed-meshheading:15281913-COS Cells,
pubmed-meshheading:15281913-Cell Line,
pubmed-meshheading:15281913-Cercopithecus aethiops,
pubmed-meshheading:15281913-Dual-Specificity Phosphatases,
pubmed-meshheading:15281913-Enzyme Activation,
pubmed-meshheading:15281913-Humans,
pubmed-meshheading:15281913-JNK Mitogen-Activated Protein Kinases,
pubmed-meshheading:15281913-MAP Kinase Kinase Kinase 4,
pubmed-meshheading:15281913-Mice,
pubmed-meshheading:15281913-Mitogen-Activated Protein Kinase 6,
pubmed-meshheading:15281913-Molecular Sequence Data,
pubmed-meshheading:15281913-Molecular Weight,
pubmed-meshheading:15281913-Mutation,
pubmed-meshheading:15281913-Osmotic Pressure,
pubmed-meshheading:15281913-Protein Tyrosine Phosphatases,
pubmed-meshheading:15281913-Substrate Specificity,
pubmed-meshheading:15281913-Transfection,
pubmed-meshheading:15281913-p38 Mitogen-Activated Protein Kinases
|
|
pubmed:year |
2004
|
|
pubmed:articleTitle |
Characterization of a novel low-molecular-mass dual-specificity phosphatase-3 (LDP-3) that enhances activation of JNK and p38.
|
|
pubmed:affiliation |
Division of Biochemical Oncology and Immunology, Institute for Genetic Medicine, Hokkaido University, Kita-15, Nishi-7, Kita-ku, Sapporo 060-0815, Japan.
|
|
pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|
