title: Dephosphorylation shows SR proteins the way out.
abstract: To address the role of the RS domain in shuttling and how it is differentially required for constitutive and alternative splicing, Lin et al. (2005 [in the November 11 issue of Molecular Cell]) employ an elegant somatic complementation system to reveal a novel phosphorylation-dependent mechanism regulating distinct recycling pathways for SR proteins during mRNP maturation.
authors.affiliation: Molecular Genetics, Department of Biomedical Sciences, School of Public Health, Ge*NY*Sis Center for Excellence in Cancer Genomics, 1 Discovery Drive, Room 220, Rensselaer, New York 12144, USA.
authors.forename: Scott A
authors.initials: SA
authors.lastname: Tenenbaum
authors.forename: Julio
authors.initials: J
authors.lastname: Aguirre-Ghiso
mesh_terms: D000818:Animals; D009687:Nuclear Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D010750:Phosphoproteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D010766:Phosphorylation; D021381:Protein Transport / Q000235:genetics; D016601:RNA-Binding Proteins; D012261:Ribonucleoproteins / Q000378:metabolism; D000068103:Serine-Arginine Splicing Factors
chemical_list: D009687:Nuclear Proteins; D010750:Phosphoproteins; D016601:RNA-Binding Proteins; D012261:Ribonucleoproteins; C026452:messenger ribonucleoprotein; D000068103:Serine-Arginine Splicing Factors