Dephosphorylation shows SR proteins the way out.
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.
Tenenbaum
Scott A
SA
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.
Aguirre-Ghiso
Julio
J
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
D009687:Nuclear Proteins; D010750:Phosphoproteins; D016601:RNA-Binding Proteins; D012261:Ribonucleoproteins; C026452:messenger ribonucleoprotein; D000068103:Serine-Arginine Splicing Factors