Linking NAADP to Ion Channel Activity: A Unifying Hypothesis

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Sci. Signal.  17 Apr 2012:
DOI: 10.1126/scisignal.2002890


Nicotinic acid adenine dinucleotide phosphate (NAADP) is a potent Ca2+-releasing second messenger that might regulate different ion channels, including the ryanodine receptor, two-pore channels, and TRP-ML1 (transient receptor potential channel, subtype mucolipin 1), a Ca2+ channel localized to lysosomes. New evidence suggests that a 22- and 23-kD pair of proteins could be the receptor for NAADP. Labeling of NAADP binding proteins was independent of overexpression or knockout of two-pore channels, indicating that two-pore channels, although regulated by NAADP, are not the NAADP receptors. I propose that NAADP binding proteins could bind to different ion channels and thus may explain how NAADP regulates diverse ion channels.

Full article available 24 April 2012, Vol. 5, Issue 221, pp. pe18