Medical College of Wisconsin
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The Molecular Basis for Ca(2+) Signalling by NAADP: Two-Pore Channels in a Complex? Messenger (Los Angel) 2012 Jun 01;1(1):63-76 PMID: 25309835 PMCID: PMC4193953

Abstract

NAADP is a potent Ca(2+) mobilizing messenger in a variety of cells but its molecular mechanism of action is incompletely understood. Accumulating evidence indicates that the poorly characterized two-pore channels (TPCs) in animals are NAADP sensitive Ca(2+)-permeable channels. TPCs localize to the endo-lysosomal system but are functionally coupled to the better characterized endoplasmic reticulum Ca(2+) channels to generate physiologically relevant complex Ca(2+) signals. Whether TPCs directly bind NAADP is not clear. Here we discuss the idea based on recent studies that TPCs are the pore-forming subunits of a protein complex that includes tightly associated, low molecular weight NAADP-binding proteins.

Author List

Marchant JS, Lin-Moshier Y, Walseth TF, Patel S

Author

Jonathan S. Marchant PhD Chair, Professor in the Cell Biology, Neurobiology and Anatomy department at Medical College of Wisconsin



View this publication's entry at the Pubmed website PMID: 25309835
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