Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2000-3-2
pubmed:abstractText
For determining cellular functions of the interferon-inducible human cytoplasmic protein P56, we undertook a Saccharomyces cerevisiae two-hybrid screen that identified Int6 as a P56-interacting protein. That the interaction also occurs in human cells was confirmed by coimmunoprecipitation and the observed cytoplasmic displacement of nuclear Int6 upon coexpression of P56. Because Int6 has been claimed to be both a cytoplasmic and a nuclear protein, we investigated the structural basis of this discrepancy. By mutational analyses, we showed that the Int6 protein contains a bipartite nuclear localization signal and a nuclear export signal at the far end of the amino terminus. The 20 amino-terminal residues of Int6, when they were attached to a different nuclear protein, were sufficient to translocate that protein to the cytoplasm. Within this region, replacement of any of the three leucine residues with alanine destroyed the function of the export signal. The specific domain of P56 that is required for its interaction with Int6 was mapped using the yeast two-hybrid assay and a mammalian coimmunoprecipitation assay. Both assays demonstrated that the C-terminal region of P56 containing three specific tetratricopeptide motifs is required for this interaction. In contrast, removal of an internal domain of P56 enhanced the interaction, as quantified by the two-hybrid assay.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/10644362-10400669, http://linkedlifedata.com/resource/pubmed/commentcorrection/10644362-1882418, http://linkedlifedata.com/resource/pubmed/commentcorrection/10644362-2118988, http://linkedlifedata.com/resource/pubmed/commentcorrection/10644362-2460741, http://linkedlifedata.com/resource/pubmed/commentcorrection/10644362-2547163, http://linkedlifedata.com/resource/pubmed/commentcorrection/10644362-3097508, http://linkedlifedata.com/resource/pubmed/commentcorrection/10644362-3360121, http://linkedlifedata.com/resource/pubmed/commentcorrection/10644362-6186990, http://linkedlifedata.com/resource/pubmed/commentcorrection/10644362-7543368, http://linkedlifedata.com/resource/pubmed/commentcorrection/10644362-7634336, http://linkedlifedata.com/resource/pubmed/commentcorrection/10644362-7642650, http://linkedlifedata.com/resource/pubmed/commentcorrection/10644362-7679242, http://linkedlifedata.com/resource/pubmed/commentcorrection/10644362-7853537, http://linkedlifedata.com/resource/pubmed/commentcorrection/10644362-8688078, http://linkedlifedata.com/resource/pubmed/commentcorrection/10644362-8709278, http://linkedlifedata.com/resource/pubmed/commentcorrection/10644362-8754816, http://linkedlifedata.com/resource/pubmed/commentcorrection/10644362-8810342, http://linkedlifedata.com/resource/pubmed/commentcorrection/10644362-8862396, http://linkedlifedata.com/resource/pubmed/commentcorrection/10644362-9207104, http://linkedlifedata.com/resource/pubmed/commentcorrection/10644362-9260927, http://linkedlifedata.com/resource/pubmed/commentcorrection/10644362-9295280, http://linkedlifedata.com/resource/pubmed/commentcorrection/10644362-9403073, http://linkedlifedata.com/resource/pubmed/commentcorrection/10644362-9417773, http://linkedlifedata.com/resource/pubmed/commentcorrection/10644362-9446600, http://linkedlifedata.com/resource/pubmed/commentcorrection/10644362-9451959, http://linkedlifedata.com/resource/pubmed/commentcorrection/10644362-9759489, http://linkedlifedata.com/resource/pubmed/commentcorrection/10644362-9861020
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0022-538X
pubmed:author
pubmed:issnType
Print
pubmed:volume
74
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1892-9
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Characterization of the interaction between the interferon-induced protein P56 and the Int6 protein encoded by a locus of insertion of the mouse mammary tumor virus.
pubmed:affiliation
Department of Molecular Biology, The Lerner Research Institute, The Cleveland Clinic Foundation, Cleveland, Ohio 44195, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.