Molecular cell · 2002
Calmodulin regulates Ca(2+)-dependent feedback inhibition of store-operated Ca(2+) influx by interaction with a site in the C terminus of TrpC1.
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Singh Brij B, Liu Xibao, Tang Jisen, Zhu Michael X, Ambudkar Indu S
Аннотация
The mechanism involved in [Ca(2+)](i)-dependent feedback inhibition of store-operated Ca(2+) entry (SOCE) is not yet known. Expression of Ca(2+)-insensitive calmodulin (Mut-CaM) but not wild-type CaM increased SOCE and decreased its Ca(2+)-dependent inactivation. Expression of TrpC1 lacking C terminus aa 664-793 (TrpC1DeltaC) also attenuated Ca(2+)-dependent inactivation of SOCE. CaM interacted with endogenous and expressed TrpC1 and with GST-TrpC1 C terminus but not with TrpC1DeltaC. Two CaM binding domains, aa 715-749 and aa 758-793, were identified. Expression of TrpC1Delta758-793 but not TrpC1Delta715-749 mimicked the effects of TrpC1DeltaC and Mut-CaM on SOCE. These data demonstrate that CaM mediates Ca(2+)-dependent feedback inhibition of SOCE via binding to a domain in the C terminus of TrpC1. These findings reveal an integral role for TrpC1 in the regulation of SOCE.
Предметные рубрики MeSH
Amino Acid SubstitutionBinding SitesCalcium ChannelsCalcium SignalingCalmodulinCell CompartmentationCell LineDNA, ComplementaryEpithelial CellsFeedbackHumansIon Channel GatingIon TransportMutagenesis, Site-DirectedPatch-Clamp TechniquesPeptide FragmentsProtein BindingProtein Interaction MappingProtein Structure, TertiaryRecombinant Fusion ProteinsSequence DeletionSubmandibular GlandTRPC Cation ChannelsTransfection