Linked Life Data

11179451

Source:http://linkedlifedata.com/resource/pubmed/id/11179451

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2001-2-22
pubmed:abstractText
The aryl hydrocarbon nuclear translocator (ARNT) protein belongs to the family of basic helix-loop-helix (HLH)-periodicity/ARNT/single-minded [Per/ARNT/Sim (PAS)] transcription factors and regulates a range of cellular processes by either homodimerizing or heterodimerizing with other basic HLH-PAS proteins. To date, it has been shown that both the HLH and PAS domains are required for aryl hydrocarbon receptor (AhR) ARNT heterodimerization and that phosphorylation of ARNT is also required for this heterodimerization. Presently, regulation of ARNT with respect to phosphorylation is poorly understood. In an earlier study, murine ARNT was shown to be a phosphoprotein, to display charge heterogeneity, and to have a shift in its predominant isoforms after heterodimerization with the AhR. It was hypothesized that this shift may represent a change in ARNT phosphorylation status. Metabolic [(32)P]orthophosphate labeling of human ARNT-transfected COS-1 cells, in conjunction with phosphoamino acid analysis, Edman degradation, and phosphopeptide mapping, demonstrated that ARNT is predominantly phosphorylated on serine residues and that serine 348 (S348) in the PAS domain is phosphorylated. Alanine and glutamic acid substitutions were used to demonstrate that loss of phosphorylation at this site did not influence AhR-mediated xenobiotic response elements-driven or ARNT-mediated class B E-box-driven signaling. Additionally, the phosphorylation pattern of ARNT was unaltered after AhR heterodimerization. Although phosphorylation of S348 did not modulate AhR-ARNT or ARNT-ARNT signaling, phosphorylation of this PAS-region serine residue may be important in other ARNT-mediated gene expression systems.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0026-895X
pubmed:author
pubmed:issnType
Print
pubmed:volume
59
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
557-66
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:11179451-Amino Acid Sequence, pubmed-meshheading:11179451-Animals, pubmed-meshheading:11179451-Aryl Hydrocarbon Receptor Nuclear Translocator, pubmed-meshheading:11179451-COS Cells, pubmed-meshheading:11179451-Cell Line, pubmed-meshheading:11179451-DNA, Complementary, pubmed-meshheading:11179451-DNA-Binding Proteins, pubmed-meshheading:11179451-Dimerization, pubmed-meshheading:11179451-Humans, pubmed-meshheading:11179451-Mutagenesis, Site-Directed, pubmed-meshheading:11179451-Phosphoamino Acids, pubmed-meshheading:11179451-Phosphoproteins, pubmed-meshheading:11179451-Phosphorylation, pubmed-meshheading:11179451-Receptors, Aryl Hydrocarbon, pubmed-meshheading:11179451-Sequence Analysis, Protein, pubmed-meshheading:11179451-Serine, pubmed-meshheading:11179451-Transcription Factors, pubmed-meshheading:11179451-Transfection
pubmed:year
2001
pubmed:articleTitle
Aryl hydrocarbon receptor (AhR)/AhR nuclear translocator (ARNT) activity is unaltered by phosphorylation of a periodicity/ARNT/single-minded (PAS)-region serine residue.
pubmed:affiliation
Department of Veterinary Science and Center for Molecular Toxicology and Carcinogenesis, The Pennsylvania State University, University Park, Pennsylvania, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.