Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5308
pubmed:dateCreated
1997-4-22
pubmed:abstractText
The transcription factor NF-AT responds to Ca2+-calcineurin signals by translocating to the nucleus, where it participates in the activation of early immune response genes. Calcineurin dephosphorylates conserved serine residues in the amino terminus of NF-AT, resulting in nuclear import. Purification of the NF-AT kinase revealed that it is composed of a priming kinase activity and glycogen synthase kinase-3 (GSK-3). GSK-3 phosphorylates conserved serines necessary for nuclear export, promotes nuclear exit, and thereby opposes Ca2+-calcineurin signaling. Because GSK-3 responds to signals initiated by Wnt and other ligands, NF-AT family members could be effectors of these pathways.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Calcineurin, http://linkedlifedata.com/resource/pubmed/chemical/Calcium, http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Calmodulin-Dependent..., http://linkedlifedata.com/resource/pubmed/chemical/Calmodulin-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP-Dependent Protein Kinases, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Glycogen Synthase Kinase 3, http://linkedlifedata.com/resource/pubmed/chemical/Glycogen Synthase Kinases, http://linkedlifedata.com/resource/pubmed/chemical/NFATC Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/NFATC1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoprotein Phosphatases, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0036-8075
pubmed:author
pubmed:issnType
Print
pubmed:day
28
pubmed:volume
275
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1930-4
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:9072970-Amino Acid Sequence, pubmed-meshheading:9072970-Animals, pubmed-meshheading:9072970-Biological Transport, pubmed-meshheading:9072970-Brain, pubmed-meshheading:9072970-COS Cells, pubmed-meshheading:9072970-Calcineurin, pubmed-meshheading:9072970-Calcium, pubmed-meshheading:9072970-Calcium-Calmodulin-Dependent Protein Kinases, pubmed-meshheading:9072970-Calmodulin-Binding Proteins, pubmed-meshheading:9072970-Cell Nucleus, pubmed-meshheading:9072970-Cloning, Molecular, pubmed-meshheading:9072970-Cyclic AMP-Dependent Protein Kinases, pubmed-meshheading:9072970-DNA-Binding Proteins, pubmed-meshheading:9072970-Glycogen Synthase Kinase 3, pubmed-meshheading:9072970-Glycogen Synthase Kinases, pubmed-meshheading:9072970-Humans, pubmed-meshheading:9072970-Molecular Sequence Data, pubmed-meshheading:9072970-NFATC Transcription Factors, pubmed-meshheading:9072970-Nuclear Proteins, pubmed-meshheading:9072970-Phosphoprotein Phosphatases, pubmed-meshheading:9072970-Phosphorylation, pubmed-meshheading:9072970-Rats, pubmed-meshheading:9072970-Recombinant Fusion Proteins, pubmed-meshheading:9072970-Signal Transduction, pubmed-meshheading:9072970-Transcription Factors, pubmed-meshheading:9072970-Transfection
pubmed:year
1997
pubmed:articleTitle
Nuclear export of NF-ATc enhanced by glycogen synthase kinase-3.
pubmed:affiliation
Howard Hughes Medical Institute, Department of Developmental Biology, Stanford University, Stanford, CA 94305, USA.
pubmed:publicationType
Journal Article