|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
8
|
|
pubmed:dateCreated |
2005-8-15
|
|
pubmed:abstractText |
SEI family proteins, p34SEI-1 and SEI-2(TRIP-Br2), are nuclear factors that are implicated in cell cycle regulation through interaction with CDK4/CyclinD and E2F-1/DP-1 complexes. Here we report that the SEI family proteins regulate transcriptional activity of p53 tumor suppressor protein. Expression of SEI-1, SEI-2 or SEI-3 strongly stimulates p53-dependent gene activation in HeLa and U2OS cells but not in p53-deficient Saos2 or p53-knockdown HeLa cells. SEI proteins possess an intrinsic transactivation activity, interact with the coactivator CREB-binding protein, and cooperate synergistically with the ING family of chromatin-associated proteins to stimulate the transactivation function of p53. Doxycycline-induced expression of SEI proteins results in activation of the p21 gene and inhibition of cell growth, but the growth arrest was not suppressed by the siRNA-mediated knockdown of the endogenous p53 protein. These results indicate that the SEI family of nuclear proteins regulates p53 transcriptional activity and a p53-independent signaling pathway leading to growth inhibition.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Chromatin,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PAG1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/SERTAD1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Protein p53
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Aug
|
|
pubmed:issn |
1356-9597
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
10
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
851-60
|
|
pubmed:dateRevised |
2008-11-21
|
|
pubmed:meshHeading |
pubmed-meshheading:16098148-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:16098148-Amino Acid Motifs,
pubmed-meshheading:16098148-Amino Acid Sequence,
pubmed-meshheading:16098148-Cell Culture Techniques,
pubmed-meshheading:16098148-Cell Cycle,
pubmed-meshheading:16098148-Cell Cycle Proteins,
pubmed-meshheading:16098148-Chromatin,
pubmed-meshheading:16098148-HeLa Cells,
pubmed-meshheading:16098148-Humans,
pubmed-meshheading:16098148-Membrane Proteins,
pubmed-meshheading:16098148-Molecular Sequence Data,
pubmed-meshheading:16098148-Nuclear Proteins,
pubmed-meshheading:16098148-Phosphoproteins,
pubmed-meshheading:16098148-RNA, Messenger,
pubmed-meshheading:16098148-Sequence Homology, Amino Acid,
pubmed-meshheading:16098148-Signal Transduction,
pubmed-meshheading:16098148-Species Specificity,
pubmed-meshheading:16098148-Time Factors,
pubmed-meshheading:16098148-Trans-Activators,
pubmed-meshheading:16098148-Transcription Factors,
pubmed-meshheading:16098148-Transcriptional Activation,
pubmed-meshheading:16098148-Tumor Suppressor Protein p53,
pubmed-meshheading:16098148-Two-Hybrid System Techniques
|
|
pubmed:year |
2005
|
|
pubmed:articleTitle |
SEI family of nuclear factors regulates p53-dependent transcriptional activation.
|
|
pubmed:affiliation |
Department of Genetics, Graduate School of Medicine, Osaka University, Suita, Osaka 565-0871, Japan.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
