Title : Mass spectrometric analysis reveals a functionally important PKA phosphorylation site in a Kir3 channel subunit.

Pub. Date : 2009 Jun

PMID : 19151997






4 Functional Relationships(s)
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1 Mutation of this residue to alanine resulted in a reduced sensitivity of Kir3.1* currents to H89 and Forskolin, confirming an in vivo role for this novel site of the Kir3.1 channel subunit in its regulation by PKA. Alanine potassium inwardly rectifying channel subfamily J member 3 Homo sapiens
2 Mutation of this residue to alanine resulted in a reduced sensitivity of Kir3.1* currents to H89 and Forskolin, confirming an in vivo role for this novel site of the Kir3.1 channel subunit in its regulation by PKA. Alanine potassium inwardly rectifying channel subfamily J member 3 Homo sapiens
3 Mutation of this residue to alanine resulted in a reduced sensitivity of Kir3.1* currents to H89 and Forskolin, confirming an in vivo role for this novel site of the Kir3.1 channel subunit in its regulation by PKA. Colforsin potassium inwardly rectifying channel subfamily J member 3 Homo sapiens
4 Mutation of this residue to alanine resulted in a reduced sensitivity of Kir3.1* currents to H89 and Forskolin, confirming an in vivo role for this novel site of the Kir3.1 channel subunit in its regulation by PKA. Colforsin potassium inwardly rectifying channel subfamily J member 3 Homo sapiens