Marchant, Jonathan S;
Gunaratne, Gihan S;
Cai, Xinjiang;
Slama, James T;
Patel, Sandip;
(2022)
NAADP-binding proteins find their identity.
Trends in Biochemical Sciences
, 47
(3)
pp. 235-249.
10.1016/j.tibs.2021.10.008.
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Abstract
Nicotinic acid adenine dinucleotide phosphate (NAADP) is a second messenger that releases Ca2+ from endosomes and lysosomes by activating ion channels called two-pore channels (TPCs). However, no NAADP-binding site has been identified on TPCs. Rather, NAADP activates TPCs indirectly by engaging NAADP-binding proteins (NAADP-BPs) that form part of the TPC complex. After a decade of searching, two different NAADP-BPs were recently identified: Jupiter microtubule associated homolog 2 (JPT2) and like-Sm protein 12 (LSM12). These discoveries bridge the gap between NAADP generation and NAADP activation of TPCs, providing new opportunity to understand and manipulate the NAADP-signaling pathway. The unmasking of these NAADP-BPs will catalyze future studies to define the molecular choreography of NAADP action.
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