Journal
JOURNAL OF CELL BIOLOGY
Volume 186, Issue 2, Pages 201-209Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200904073
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Funding
- Biotechnology and Biological Sciences Research Council [BB/D018110/1, BB/G013721/1]
- Wellcome Trust [VS/07/UCL/A7]
- National Institutes of Health [HL90804, GM08879]
- American Heart Association [NS18710, HL51314]
- Biotechnology and Biological Sciences Research Council [BB/G013721/1, BB/D018110/1] Funding Source: researchfish
- BBSRC [BB/G013721/1, BB/D018110/1] Funding Source: UKRI
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Nicotinic acid adenine dinucleotide phosphate (NAADP) is a widespread and potent calcium-mobilizing messenger that is highly unusual in activating calcium channels located on acidic stores. However, the molecular identity of the target protein is unclear. In this study, we show that the previously uncharacterized human two-pore channels (TPC1 and TPC2) are endolysosomal proteins, that NAADP-mediated calcium signals are enhanced by overexpression of TPC1 and attenuated after knockdown of TPC1, and that mutation of a single highly conserved residue within a putative pore region abrogated calcium release by NAADP. Thus, TPC1 is critical for NAADP action and is likely the long sought after target channel for NAADP.
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