Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2-3
pubmed:dateCreated
2004-6-4
pubmed:abstractText
Okadaic acid (OA) is a protein phosphatase (PP) inhibitor and induces hyperphosphorylation of p53. We investigated whether the inhibition of PP1 by OA promotes the phosphorylation of the serine 15 of p53. In vitro dephosphorylation assay showed that PP1 dephosphorylated ultraviolet C (UVC)-induced phospho-ser15 of p53, and that OA treatment inhibited it. One of the PP1 regulators, growth arrest and DNA damage 34 (GADD34), disturbed PP1 binding with p53, interfered with the dephosphorylation of p53 and increased the amount of phospho-p53 after UVC-treatment. This report provides the first evidence that PP1, but not PP2A, dephosphorylates phospho-serine 15 of p53.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Differentiation, http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Polyomavirus Transforming, http://linkedlifedata.com/resource/pubmed/chemical/CDKN1A protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Cdkn1a protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Cyclin-Dependent Kinase Inhibitor..., http://linkedlifedata.com/resource/pubmed/chemical/Cyclins, http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors, http://linkedlifedata.com/resource/pubmed/chemical/Eukaryotic Initiation Factor-2, http://linkedlifedata.com/resource/pubmed/chemical/Methyl Methanesulfonate, http://linkedlifedata.com/resource/pubmed/chemical/Okadaic Acid, http://linkedlifedata.com/resource/pubmed/chemical/PPP1R15A protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoprotein Phosphatases, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoserine, http://linkedlifedata.com/resource/pubmed/chemical/Ppp1r15a protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Protein Phosphatase 1, http://linkedlifedata.com/resource/pubmed/chemical/Protein Phosphatase 2, http://linkedlifedata.com/resource/pubmed/chemical/Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Protein p53
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
4
pubmed:volume
567
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
171-4
pubmed:dateRevised
2011-4-12
pubmed:meshHeading
pubmed-meshheading:15178317-Animals, pubmed-meshheading:15178317-Antigens, Differentiation, pubmed-meshheading:15178317-Antigens, Polyomavirus Transforming, pubmed-meshheading:15178317-Cell Cycle Proteins, pubmed-meshheading:15178317-Cell Line, pubmed-meshheading:15178317-Cyclin-Dependent Kinase Inhibitor p21, pubmed-meshheading:15178317-Cyclins, pubmed-meshheading:15178317-DNA Damage, pubmed-meshheading:15178317-Embryo, Mammalian, pubmed-meshheading:15178317-Enzyme Inhibitors, pubmed-meshheading:15178317-Eukaryotic Initiation Factor-2, pubmed-meshheading:15178317-Fibroblasts, pubmed-meshheading:15178317-Humans, pubmed-meshheading:15178317-Methyl Methanesulfonate, pubmed-meshheading:15178317-Mice, pubmed-meshheading:15178317-Mice, Knockout, pubmed-meshheading:15178317-Okadaic Acid, pubmed-meshheading:15178317-Phosphoprotein Phosphatases, pubmed-meshheading:15178317-Phosphorylation, pubmed-meshheading:15178317-Phosphoserine, pubmed-meshheading:15178317-Protein Phosphatase 1, pubmed-meshheading:15178317-Protein Phosphatase 2, pubmed-meshheading:15178317-Proteins, pubmed-meshheading:15178317-Tumor Suppressor Protein p53, pubmed-meshheading:15178317-Ultraviolet Rays
pubmed:year
2004
pubmed:articleTitle
Protein phosphatase 1, but not protein phosphatase 2A, dephosphorylates DNA-damaging stress-induced phospho-serine 15 of p53.
pubmed:affiliation
Department of Basic Gerontology, National Institute for Longevity Sciences, 36-3 Gengo, Morioka-cho, Obu, Aichi 474-8522, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't