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Updated: Jan 4, 2026

Single-molecule Super-resolution Imaging of Phosphatidylinositol 4,5-bisphosphate in the Plasma Membrane with Novel Fluorescent Probes
Published on: October 15, 2016
Wasted TMEM16A channels are rescued by phosphatidylinositol 4,5-bisphosphate
Jorge Arreola1, H Criss Hartzell2
1Physics Institute, Universidad Autónoma de San Luis Potosí, Ave. Dr. M. Nava #6, San Luis Potosí, SLP 78290, Mexico.
Abstract:
Recently there has been a flurry of interest in the regulation of the homo-dimeric calcium-activated chloride channel ANO1 (also known as TMEM16A) by phosphatidylinositol (4,5)-bisphosphate (PI(4,5)P2). These recent studies show that upon Ca2+ binding, PI(4,5)P2 cooperates to maintain the conductive state of ANO1. PI(4,5)P2 does so by binding to sites or modules on the protein's cytosolic side. These findings add a new function to the PI(4,5)P2 repertoire and a new dimension to ANO1 gating.
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