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Phosphatidylinositol 4,5-bisphosphate (PIP2 ) is necessary for the function of various ion channels. The potassium channel, IKs , is important for cardiac repolarization and requires PIP2 to activate. Here we show that the auxiliary subunit of IKs , KCNE1, increases PIP2 sensitivity 100-fold over channels formed by the pore-forming KCNQ1 subunits alone, which effectively amplifies current because native PIP2 levels in the membrane are insufficient to activate all KCNQ1 channels. A juxtamembranous site in the KCNE1 C terminus is a key structural determinant of PIP2 sensitivity. Long QT syndrome associated mutations of this site lower PIP2 affinity, resulting in reduced current. Application of exogenous PIP2 to these mutants restores wild-type channel activity. These results reveal a vital role of PIP2 for KCNE1 modulation of IKs channels that may represent a common mechanism of auxiliary subunit modulation of many ion channels.

KCNE1 enhances phosphatidylinositol 4,5-bisphosphate (PIP 2 ) sensitivity of I Ks to modulate channel activity

KCNE1 enhances phosphatidylinositol 4,5-bisphosphate (PIP ₂ ) sensitivity of I _Ks to modulate channel activity