Abstract
TMEM16A is a Ca2+-activated Cl− channel that regulates diverse cellular functions including fluid secretion, neuronal excitability and smooth muscle contraction. TMEM16A is activated by cytosolic Ca2+ and modulated by binding of the signaling lipid, PIP2. However, it remains elusive how PIP2 binds the channel and how the binding affects molecular events underlying transport in the protein. Here, we use extended molecular dynamics (MD) simulations coupled with electrophysiology, mutagenesis, and functional assays, to characterize PIP2 binding modes and sites in TMEM16A and the conformational response of the channel to PIP2 binding.
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