title: Phosphorylation control of nuclear receptors.
abstract: Most transcription factors including nuclear receptors (NRs) act as sensors of the extracellular and intracellular compartments. As such, NRs serve as integrating platforms for a variety of stimuli and are targets for Post-translational modifications such as phosphorylations. During the last decade, knowledge of NRs phosphorylation advanced considerably because of the emergence of new technologies. Indeed, the development of a wide range of phosphorylation site databases, high accuracy mass spectrometry, and phospho-specific antibodies allowed the identification of multiple novel phosphorylation sites in NRs. New and improved methods also emerge to connect these data with the downstream consequences of phosphorylation on NRs structure (computational prediction, NMR), intracellular localization (FRAP), interaction with coregulators (proteomics, FRET, FLIM), and affinity for DNA (ChIP, ChIP-seq, FRAP). In the future, such integrated strategies should provide data with a treasure-trove of information about the integration of numerous signaling events by NRs.
authors.affiliation: Department of Functional Denomics, Institut de Genetique et de Biologie Molecularie et Cellulaire, Strasbourg, France.
authors.forename: Sébastien
authors.initials: S
authors.lastname: Lalevée
authors.forename: Christine
authors.initials: C
authors.lastname: Ferry
authors.forename: Cécile
authors.initials: C
authors.lastname: Rochette-Egly
mesh_terms: D000818:Animals; D006801:Humans; D042541:Intracellular Space / Q000378:metabolism; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism; D021381:Protein Transport; D018160:Receptors, Cytoplasmic and Nuclear / Q000737:chemistry / Q000378:metabolism*; D014158:Transcription, Genetic
chemical_list: D018160:Receptors, Cytoplasmic and Nuclear; D011494:Protein Kinases