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J Biol Chem, Vol. 274, Issue 17, 11643-11646, April 23, 1999
From the Department of Biology, Georgia State University,
Atlanta, Georgia 30303-4010
Kir2.3 plays an important part in the maintenance
of membrane potential in neurons and myocardium. Identification of
intracellular signaling molecules controlling this channel thus may
lead to an understanding of the regulation of membrane excitability. To determine whether Kir2.3 is modulated by direct phosphorylation of its
channel protein and identify the phosphorylation site of protein kinase
C (PKC), we performed experiments using several recombinant and mutant
Kir2.3 channels. Whole-cell Kir2.3 currents were inhibited by phorbol
12-myristate 13-acetate (PMA) in Xenopus oocytes. When the
N-terminal region of Kir2.3 was replaced with that of Kir2.1, another
member in the Kir2 family that is insensitive to PMA, the chimerical
channel lost its PMA sensitivity. However, substitution of the C
terminus was ineffective. Four potential PKC phosphorylation sites in
the N terminus were studied by comparing mutations of serine or
threonine with their counterpart residues in Kir2.1. Whereas
substitutions of serine residues at positions 5, 36, and 39 had no
effect on the channel sensitivity to PMA, mutation of threonine 53 completely eliminated the channel response to PMA. Interestingly,
creation of this threonine residue at the corresponding position (I79T)
in Kir2.1 lent the mutant channel a PMA sensitivity almost identical to
the wild-type Kir2.3. These results therefore indicate that Kir2.3 is
directly modulated by PKC phosphorylation of its channel protein and
threonine 53 is the PKC phosphorylation site in Kir2.3.
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