| First Author | Mallmann RT | Year | 2013 |
| Journal | Sci Rep | Volume | 3 |
| Pages | 1777 | PubMed ID | 23648579 |
| Mgi Jnum | J:207256 | Mgi Id | MGI:5554988 |
| Doi | 10.1038/srep01777 | Citation | Mallmann RT, et al. (2013) Tetraspanin-13 modulates voltage-gated CaV2.2 Ca2+ channels. Sci Rep 3:1777 |
| abstractText | Integration of voltage-gated Ca(2+) channels in a network of protein-interactions is a crucial requirement for proper regulation of channel activity. In this study, we took advantage of the specific properties of the yeast split-ubiquitin system to search for and characterize so far unknown interaction partners of CaV2 Ca(2+) channels. We identified tetraspanin-13 (TSPAN-13) as an interaction partner of the alpha1 subunit of N-type CaV2.2, but not of P/Q-type CaV2.1 or L- and T-type Ca(2+) channels. Interaction could be located between domain IV of CaV2.2 and transmembrane segments S1 and S2 of TSPAN-13. Electrophysiological analysis revealed that TSPAN-13 specifically modulates the efficiency of coupling between voltage sensor activation and pore opening of the channel and accelerates the voltage-dependent activation and inactivation of the Ba(2+) current through CaV2.2. These data indicate that TSPAN-13 might regulate CaV2.2 Ca(2+) channel activity in defined synaptic membrane compartments and thereby influences transmitter release. |
