Tetraspanin-13 modulates voltage-gated Cav2.2 Ca2+ channels
Contributors: Wilmes, Thomas 1979- Verfasser; Lichvarova, Lucia Verfasser; Bührer, Anja Verfasser; Lohmüller, Barbara Verfasser; Castonguay, Jan Richard Verfasser; Klugbauer, Axel Verfasser; Albert-Ludwigs-Universität Freiburg Institut für Experimentelle und Klinische Pharmakologie und Toxikologie; Albert-Ludwigs-Universität Freiburg Fakultät für Biologie; Albert-Ludwigs-Universität Freiburg Fakultät für Chemie und Pharmazie; Albert-Ludwigs-Universität Freiburg
Publisher: Universität
Published: 2013
Place of publication: Freiburg
Language: eng
Subjects: Krebs; Onkologie
Description: Abstract: Integration of voltage-gated Ca2+ 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 Ca2+ channels. We identified tetraspanin-13 (TSPAN-13) as an interaction partner of the α1 subunit of N-type CaV2.2, but not of P/Q-type CaV2.1 or L- and T-type Ca2+ 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 Ba2+ current through CaV2.2. These data indicate that TSPAN-13 might regulate CaV2.2 Ca2+ channel activity in defined synaptic membrane compartments and thereby influences transmitter release
Notes: Scientific reports. 3 (2013), 1777, DOI 10.1038/srep01777, issn: 2045-2322

IN COPYRIGHT http://rightsstatements.org/page/InC/1.0 rs

Archivierung/Langzeitarchivierung gewährleistet