A potential site of functional modulation by protein kinase A in the cardiac Ca2+ channel alpha(1C) subunit

被引：71

作者：

Perets, T ^{[1
]}

Blumenstein, Y ^{[1
]}

Shistik, E ^{[1
]}

Lotan, I ^{[1
]}

Dascal, N ^{[1
]}

机构：

[1] TEL AVIV UNIV,SACKLER SCH MED,DEPT PHYSIOL & PHARMACOL,RAMAT AVIV,ISRAEL

来源：

FEBS LETTERS | 1996年 / 384卷 / 02期

关键词：

calcium channel; protein kinase A; modulation; mutation; subunit; Xenopus oocyte;

D O I：

10.1016/0014-5793(96)00303-1

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The well-characterized enhancement of the cardiac Ca2+ L-type current by protein kinase A (PKA) is not observed when the corresponding channel is expressed in Xenopus oocytes, possibly because it is fully phosphorylated in the basal state. However, the activity of the expressed channel is reduced by PKA inhibitors. Using this paradigm as an assay to search for PKA sites relevant to channel modulation, rye have found that mutation of serine 1928 of the alpha(1C) subunit to alanine abolishes the modulation of the expressed channel by PKA inhibitors. This effect was independent of the presence of the beta subunit, Phosphorylation of serine 1928 of alpha(1C) may mediate the modulatory effect of PKA on the cardiac voltage-dependent Ca2+ channel.

引用

页码：189 / 192

页数：4

共 44 条

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