Voltage-gated Kv7 (KCNQ) potassium channels underlie important K⁺ currents, including the neuronal M current and cardiac I_Ks. Recent work of several groups suggests high sensitivity of Kv7 channels to membrane phosphatidylinositol 4,5-bisphosphate (PIP₂) and puts forward the hypothesis that PIP₂ depletion underlie modulation of these channels by some G_g/11-coupled receptors, including muscarinic acetylcholine M1 and angiotensin II AT1 receptors. In this pathway, receptor stimulation results in activation of phospholipase C (PLC), which hydrolyzes PIP₂ into membrane-bound diacylglycerol (DAG) and soluble inositol trisphosphate (IP3) (reviewed by Delmas and Brown, 2005). Recent single-channel experiments suggest that PIP₂ acts as a stabilizer of channel opening by favouring the allosteric conformational change that opens the channel, such that channel open probability (P_o) is increased on the voltage-independent manner. It has also been demonstrated that different Kv7 channels display highly differential apparent affinity for PIP₂ (Li et al. 2005) and that different PIP₂ affinity may underlie highly diverse P_o of individual Kv7 channels in intact cells (for example both maximal P_o in cell-attached patches and apparent PIP₂ affinity of Kv7.4 are about 10 times lover then that of Kv7.3). I will discuss experiments that have led up to the establishment of the concept of PIP₂-sensitivity of Kv7 channels, its implications in health and disease as well as some unresolved problems in the field.