2010 - Characterization of two pore channel 2 (TPCN2) -mediated Ca2+ currents in isolated lysosomes

  Port-a-Patch publication in The Journal of Biological Chemistry (2010)

Authors:
Schieder M., Rötzer K., Brüggemann A., Biel M., Wahl-Schott C.A.

Journal: 
The Journal of Biological Chemistry (2010) 285(28):21219–21222

Abstract: 

Two-pore channels (TPCNs) have been proposed to form lysosomal Ca²⁺ release channels that are activated by nicotinic acid adenine dinucleotide phosphate. Here, we employ a glass chip-based method to record for the first time nicotinic acid adenine dinucleotide phosphate -dependent currents through a two-pore channel (TPCN2) from intact lysosomes. We show that TPCN2 is a highly selective Ca²⁺ channel that is regulated by intralysosomal pH. Using site-directed mutagenesis, we identify an amino acid residue in the putative pore region that is crucial for conferring high Ca²⁺ selectivity. Our glass chip-based method will provide electrophysiological access not only to lysosomal TPCN channels but also to a broad range of other intracellular ion channels.

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