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rdf:type |
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lifeskim:mentions |
umls-concept:C0012854,
umls-concept:C0018270,
umls-concept:C0033684,
umls-concept:C0086418,
umls-concept:C0237477,
umls-concept:C0292369,
umls-concept:C0542341,
umls-concept:C0812273,
umls-concept:C1422599,
umls-concept:C1704461,
umls-concept:C2261644
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pubmed:issue |
31
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pubmed:dateCreated |
2002-7-29
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pubmed:abstractText |
The growth arrest and DNA damage-inducible protein (GADD34) mediates growth arrest and apoptosis in response to DNA damage, negative growth signals, and protein malfolding. GADD34 binds to protein phosphatase-1 (PP1) and can attenuate translational elongation of key transcriptional factors through dephosphorylation of eukaryotic initiation factor-2alpha. We reported previously that the human trithorax leukemia fusion protein (HRX) can bind to GADD34 and abrogate GADD34-mediated apoptosis in response to UV irradiation. We found that hSNF5/INI1, a component of the hSWI/SNF chromatin remodeling complex, also binds to GADD34 and can coexist with GADD34 and HRX fusion proteins as a trimolecular complexes in vivo. In the present report, we demonstrate that hSNF5/INI1 binds to GADD34 in part through the PP1 docking site within a domain homologous to herpes simplex virus-1 ICP34.5. We found that hSNF5/INI1 can bind PP1 independently and weakly stimulate its phosphatase activity in solution and in complex with GADD34. hSNF5/INI1 and PP1 do not compete for binding to GADD34 but rather form a stable heterotrimeric complex with GADD34. We also show that Epstein-Barr nuclear protein 2, which binds hSNF5/INI1, can disrupt hSNF5/INI1 binding to GADD34 and partially reverse the GADD34-mediated growth suppression function in Ha-ras expressing HIH-3T3 (3T3-ras) cells. These results implicate hSNF5/INI1 in the function of GADD34 and suggest that hSNF5/INI1 may regulate PP1 activity in vivo.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Differentiation,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Chromosomal Proteins, Non-Histone,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PPP1R15A protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoprotein Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Ppp1r15a protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Phosphatase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SMARCB1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Smarcb1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
2
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pubmed:volume |
277
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
27706-15
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pubmed:dateRevised |
2011-4-12
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pubmed:meshHeading |
pubmed-meshheading:12016208-3T3 Cells,
pubmed-meshheading:12016208-Amino Acid Sequence,
pubmed-meshheading:12016208-Animals,
pubmed-meshheading:12016208-Antigens, Differentiation,
pubmed-meshheading:12016208-Binding Sites,
pubmed-meshheading:12016208-Cell Cycle Proteins,
pubmed-meshheading:12016208-Cell Division,
pubmed-meshheading:12016208-Cell Line,
pubmed-meshheading:12016208-Cell Survival,
pubmed-meshheading:12016208-Chromosomal Proteins, Non-Histone,
pubmed-meshheading:12016208-Cloning, Molecular,
pubmed-meshheading:12016208-DNA Damage,
pubmed-meshheading:12016208-DNA-Binding Proteins,
pubmed-meshheading:12016208-Humans,
pubmed-meshheading:12016208-Mice,
pubmed-meshheading:12016208-Molecular Sequence Data,
pubmed-meshheading:12016208-Peptide Fragments,
pubmed-meshheading:12016208-Phosphoprotein Phosphatases,
pubmed-meshheading:12016208-Protein Phosphatase 1,
pubmed-meshheading:12016208-Proteins,
pubmed-meshheading:12016208-Recombinant Fusion Proteins,
pubmed-meshheading:12016208-Recombinant Proteins,
pubmed-meshheading:12016208-Transcription Factors,
pubmed-meshheading:12016208-Transfection
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pubmed:year |
2002
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pubmed:articleTitle |
The human SNF5/INI1 protein facilitates the function of the growth arrest and DNA damage-inducible protein (GADD34) and modulates GADD34-bound protein phosphatase-1 activity.
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pubmed:affiliation |
Division of Medical Oncology, Department of Medicine, Veterans Administration Puget Sound Health Care System, Seattle Division, Seattle, Washington 98108, USA. danielw@u.washington.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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