Faculty Collaboration Database

The Molecular Basis for Ca²⁺ Signalling by NAADP: Two-Pore Channels in a Complex? Messenger (Los Angel) 2012 Jun 01;1(1):63-76

Date

06/01/2012

Pubmed ID

25309835

Pubmed Central ID

PMC4193953

DOI

10.1166/msr.2012.1003

Abstract

NAADP is a potent Ca²⁺ 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 Ca²⁺-permeable channels. TPCs localize to the endo-lysosomal system but are functionally coupled to the better characterized endoplasmic reticulum Ca²⁺ channels to generate physiologically relevant complex Ca²⁺ 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