Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2002-5-1
pubmed:abstractText
Networks of protein interactions coordinate cellular functions. We describe a bimolecular fluorescence complementation (BiFC) assay for determination of the locations of protein interactions in living cells. This approach is based on complementation between two nonfluorescent fragments of the yellow fluorescent protein (YFP) when they are brought together by interactions between proteins fused to each fragment. BiFC analysis was used to investigate interactions among bZIP and Rel family transcription factors. Regions outside the bZIP domains determined the locations of bZIP protein interactions. The subcellular sites of protein interactions were regulated by signaling. Cross-family interactions between bZIP and Rel proteins affected their subcellular localization and modulated transcription activation. These results attest to the general applicability of the BiFC assay for studies of protein interactions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/I-kappa B Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Ligases, http://linkedlifedata.com/resource/pubmed/chemical/Luminescent Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances, http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B, http://linkedlifedata.com/resource/pubmed/chemical/NF-kappaB inhibitor alpha, http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments, http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-fos, http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-jun, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/guanosine 3',5'-polyphosphate..., http://linkedlifedata.com/resource/pubmed/chemical/yellow fluorescent protein, Bacteria
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1097-2765
pubmed:author
pubmed:issnType
Print
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
789-98
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:11983170-3T3 Cells, pubmed-meshheading:11983170-Alternative Splicing, pubmed-meshheading:11983170-Animals, pubmed-meshheading:11983170-Bacterial Proteins, pubmed-meshheading:11983170-COS Cells, pubmed-meshheading:11983170-Cell Compartmentation, pubmed-meshheading:11983170-Cercopithecus aethiops, pubmed-meshheading:11983170-DNA-Binding Proteins, pubmed-meshheading:11983170-Dimerization, pubmed-meshheading:11983170-Fluorescence, pubmed-meshheading:11983170-HeLa Cells, pubmed-meshheading:11983170-Humans, pubmed-meshheading:11983170-I-kappa B Proteins, pubmed-meshheading:11983170-Leucine Zippers, pubmed-meshheading:11983170-Ligases, pubmed-meshheading:11983170-Luminescent Proteins, pubmed-meshheading:11983170-Macromolecular Substances, pubmed-meshheading:11983170-Mice, pubmed-meshheading:11983170-Microscopy, Fluorescence, pubmed-meshheading:11983170-NF-kappa B, pubmed-meshheading:11983170-Peptide Fragments, pubmed-meshheading:11983170-Protein Interaction Mapping, pubmed-meshheading:11983170-Protein Structure, Tertiary, pubmed-meshheading:11983170-Protein Transport, pubmed-meshheading:11983170-Proto-Oncogene Proteins c-fos, pubmed-meshheading:11983170-Proto-Oncogene Proteins c-jun, pubmed-meshheading:11983170-Recombinant Fusion Proteins, pubmed-meshheading:11983170-Sequence Deletion, pubmed-meshheading:11983170-Subcellular Fractions, pubmed-meshheading:11983170-Transcription, Genetic, pubmed-meshheading:11983170-Transfection
pubmed:year
2002
pubmed:articleTitle
Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation.
pubmed:affiliation
Howard Hughes Medical Institute and Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor, MI 48109, USA.
pubmed:publicationType
Journal Article