| First Author | Schieder M | Year | 2010 |
| Journal | J Biol Chem | Volume | 285 |
| Issue | 28 | Pages | 21219-22 |
| PubMed ID | 20495006 | Mgi Jnum | J:175340 |
| Mgi Id | MGI:5285159 | Doi | 10.1074/jbc.C110.143123 |
| Citation | Schieder M, et al. (2010) Characterization of two-pore channel 2 (TPCN2)-mediated Ca2+ currents in isolated lysosomes. J Biol Chem 285(28):21219-22 |
| abstractText | Two-pore channels (TPCNs) have been proposed to form lysosomal Ca(2+) 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 Ca(2+) 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 Ca(2+) 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. |
