| RRC ID |
38402
|
| 著者 |
Sudo T, Maruyama M, Osada H.
|
| タイトル |
p62 functions as a p38 MAP kinase regulator.
|
| ジャーナル |
Biochem Biophys Res Commun
|
| Abstract |
By screening a HeLa cDNA library to isolate genes encoding p38-regulating proteins, we have isolated two independent clones which encode the binding proteins to p38. We have found that both of these cDNA clones encode p62, first identified as a phosphorylation independent p56(lck) SH2 domain binding protein. Recent studies also indicate that p62 interacts with atypical PKCs to anchor them to intracellular membranes and with RIP to mediate signals to NF-kappaB through atypical PKCs. Moreover, p62 is shown to be involved in the transcriptional regulation via SV40 enhancer and to serve as a coactivator of an orphan nuclear hormone receptor. A coimmunoprecipitation assay shows its enhanced association in HeLa cells after stimulations such as sorbitol and anisomycin. An indirect immunofluorescence study indicates that p62 colocalizes with p38 in the nucleus in response to the stimulation. And in vitro kinase assays using MBP, but not ATF-2, as a substrate show that p62 enhances p38 activities in a dose-dependent manner. Together, these results demonstrate that p62 plays roles not only as an anchor but also as a regulator for the p38 kinase activity.
|
| 巻・号 |
269(2)
|
| ページ |
521-5
|
| 公開日 |
2000-3-16
|
| DOI |
10.1006/bbrc.2000.2333
|
| PII |
S0006-291X(00)92333-7
|
| PMID |
10708586
|
| MeSH |
Adaptor Proteins, Signal Transducing / physiology*
Base Sequence
Calcium-Calmodulin-Dependent Protein Kinases / metabolism*
DNA Primers
Fluorescent Antibody Technique, Indirect
HeLa Cells
Humans
Mitogen-Activated Protein Kinases*
Myelin Basic Protein / metabolism
Phosphorylation
Sequestosome-1 Protein
Subcellular Fractions / metabolism
p38 Mitogen-Activated Protein Kinases
|
| IF |
2.985
|
| 引用数 |
33
|
|
WOS 分野
|
BIOPHYSICS
BIOCHEMISTRY & MOLECULAR BIOLOGY
|
| リソース情報 |
| 遺伝子材料 |
pcDNA3Flag-p38 (RDB08160)
pGEX-p38 (RDB08164)
pBK-CMVp62Flag (RDB08189). |
