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Báo cáo khoa học: The interaction between casein kinase Ia and 14-3-3 is phosphorylation dependent

We have previously shown that casein kinase (CK) Iafrom mammalian brain phosphorylates 14-3-3fandsisoforms on residue 233. In the present study, we show that CKIaassociates with 14-3-3 bothin vitro andin vivo. The interaction between CKIaand 14-3-3 is dependent on CKIaphosphor-ylation, unlike centaurin-a1 (also known as ADAP1), which binds to unphosphorylated CKIaon the same region. | ỊFEBS Journal The interaction between casein kinase Ia and 14-3-3 is phosphorylation dependent Samuel Clokie Helen Falconer Shaun Mackief Thierry DuboisỊ and Alastair Aitken Institute of StructuralBiology Edinburgh University UK Keywords 14-3-3 centaurin alpha CKI IVTT phosphorylation Correspondence A. Aitken Institute of StructuralBiology Edinburgh University Kings Buildings Edinburgh EH9 3JR UK Fax 44 131 650 5357 Tel 44 131 650 5357 E-mail alastair.aitken@ed.ac.uk Present address National Institute of Child Health and Human Development NationalInstitutes of Health Bethesda MD USA fPsychiatric Genetics Section Medical Genetics Section University of Edinburgh Western General Hospital Edinburgh UK ỊDépartement de Transfert Laboratoire de Signalisation Institut Curie Hopital Saint-Louis Paris France We have previously shown that casein kinase CK Ia from mammalian brain phosphorylates 14-3-3 f and s isoforms on residue 233. In the present study we show that CKIa associates with 14-3-3 both in vitro and in vivo. The interaction between CKIa and 14-3-3 is dependent on CKIa phosphorylation unlike centaurin-a1 also known as ADAP1 which binds to unphosphorylated CKIa on the same region. CKIa preferentially interacts with mammalian g and c 14-3-3 isoforms and peptides that bind to the 14-3-3 binding pocket prevent this interaction. The region containing Ser218 in this CKIa binding site was mutated and the interaction between CKIa and 14-3-3 was reduced. We subsequently identified a second phosphorylation-dependent 14-3-3 binding site within CKIa containing Ser242 that may be the principal site of interaction. We also show that both fission and budding yeast CKI kinase homologues phosphorylate mammalian and budding yeast BMH1 and BMH2 14-3-3 at the equivalent site. Structured digital abstract A list of the large number of protein-protein interactions described in this article is available via the MINT article ID MINT-7264069 Received 1 July 2009 revised 31 August 2009 .