Coassembly of TRP and TRPL produces a distinct store-operated conductance.
The Drosophila retinal-specific protein, TRP (transient receptor potential), is the founding member of a family of store-operated channels (SOCs) conserved from C. elegans to humans. In vitro studies indicate that TRP is a SOC, but that the related retinal protein, TRPL, is constitutively active. In the current work, we report ... that coexpression of TRP and TRPL leads to a store-operated, outwardly rectifying current distinct from that owing to either TRP or TRPL alone. TRP and TRPL interact directly, indicating that the TRP-TRPL-dependent current is mediated by heteromultimeric association between the two subunits. We propose that the light-activated current in photoreceptor cells is produced by a combination of TRP homo- and TRP-TRPL heteromultimers.
Mesh Terms:
Animals, Calcium Channels, Calmodulin-Binding Proteins, Cell Membrane, Cells, Cultured, Drosophila, Drosophila Proteins, Electric Conductivity, Humans, Membrane Proteins, Patch-Clamp Techniques, Photoreceptor Cells, Invertebrate, Precipitin Tests, Protein Binding, Protein Structure, Tertiary, TRPC Cation Channels, Transient Receptor Potential Channels, Yeasts
Animals, Calcium Channels, Calmodulin-Binding Proteins, Cell Membrane, Cells, Cultured, Drosophila, Drosophila Proteins, Electric Conductivity, Humans, Membrane Proteins, Patch-Clamp Techniques, Photoreceptor Cells, Invertebrate, Precipitin Tests, Protein Binding, Protein Structure, Tertiary, TRPC Cation Channels, Transient Receptor Potential Channels, Yeasts
Cell
Date: Jun. 27, 1997
PubMed ID: 9215637
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