Description: Alternative splicing removes the IQ motif of Voltage-dependent L-type calcium channel subunit alpha-1D (Cacna1d) abrogating binding to Calmodulin (Calm1). CaV1.3IQdelta (IQ-deleted Isoform CACN4B of Voltage-dependent L-type calcium channel subunit alpha-1D (Cacna1d)) channels exhibit a lack of calcium-dependent inactivation. CaV1.3IQdelta channel immunoreactivity was preferentially localised to cochlear outer hair cells (OHCs), whereas that of CaV1.3IQfull channels (IQ-possessing Isoform CACN4A of Voltage-dependent L-type calcium channel subunit alpha-1D (Cacna1d)) labelled inner hair cells (IHCs).
Participants: (1) Voltage-dependent L-type calcium channel subunit alpha-1D (Cacna1d) (2) Calmodulin (Calm1)
(1) Alternative splicing of the Ca(v)1.3 channel IQ domain, a molecular switch for Ca2+-dependent inactivation within auditory hair cells.Shen et al. J. Neurosci. (2006) (2) Functional characterization of alternative splicing in the C terminus of L-type CaV1.3 channels.Tan et al. J. Biol. Chem. (2011)
Other switches involving participantsCalmodulin (Calm1) - 2 more (view)Other switches involving interfacesEF-hand domain pair - 5 more (view)LIG_IQ - 2 more (view)
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