TAILIEUCHUNG - Báo cáo khoa học: Identification of the structural determinant responsible for the phosphorylation of G-protein activated potassium channel 1 by cAMP-dependent protein kinase

Besides being activated by G-proteinb⁄c subunits, G-protein activated potassium channels (GIRKs) are regulated by cAMP-dependent protein kinase. Back-phosphorylation experiments have revealed that the GIRK1 subunit is phosphorylatedin vivo upon protein kinase A activation inXeno-pusoocytes, whereas phosphorylation was eliminated when protein kinase A was blocked. | ễFEBS Journal Identification of the structural determinant responsible for the phosphorylation of G-protein activated potassium channel 1 by cAMP-dependent protein kinase Carmen Mullner Bibiane Steinecker Astrid Gorischek and Wolfgang Schreibmayer Department of Biophysics Center for PhysiologicalMedicine MedicalUniversity of Graz Austria Keywords GiRk IK Ach PKA Correspondence W. Schreibmayer Department of Biophysics Center for PhysiologicalMedicine Medical University of Graz Harrachgasse 21 4 A-8010 Graz Austria Tel 43 316 380 4155 Fax 43 316 380 9660 E-mail Received 17 June 2009 revised 17 August 2009 accepted 24 August 2009 doi Besides being activated by G-protein p ỵ subunits G-protein activated potassium channels GIRKs are regulated by cAMP-dependent protein kinase. Back-phosphorylation experiments have revealed that the GIRK1 subunit is phosphorylated in vivo upon protein kinase A activation in Xeno-pus oocytes whereas phosphorylation was eliminated when protein kinase A was blocked. In vitro phosphorylation experiments using truncated versions of GIRK1 revealed that the structural determinant is located within the distant unique cytosolic C-terminus of GIRK1. Serine 385 serine 401 and threonine 407 were identified to be responsible for the incorporation of radioactive 32P into the protein. Furthermore the functional effects of cAMP injections into oocytes on currents produced by GIRK1 homooligomers were significantly reduced when these three amino acids were mutated. The data obtained in the present study provide information about the structural determinants that are responsible for protein kinase A phosphorylation and the regulation of GIRK channels. Structured digital abstract MINT-7260296 MINT-7260317 MINT-7260333 MINT-7260347 MINT-7260361 MINT-7260270 PKA-cs uniprotkb P00517 phosphorylates MI 0217 Gỉrkl uniprotkb P63251 by protein kinase assay MI 0424 Introduction G-protein activated .

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