Abstract
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.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Calcium Channels / chemistry
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Calcium Channels / isolation & purification
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Calcium Channels / metabolism*
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Calmodulin-Binding Proteins / chemistry
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Calmodulin-Binding Proteins / isolation & purification
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Calmodulin-Binding Proteins / metabolism*
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Cell Membrane / chemistry
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Cells, Cultured
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Drosophila / chemistry
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Drosophila / physiology
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Drosophila Proteins*
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Electric Conductivity
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Humans
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Membrane Proteins / chemistry
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Membrane Proteins / isolation & purification
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Membrane Proteins / metabolism*
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Patch-Clamp Techniques
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Photoreceptor Cells, Invertebrate / physiology
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Precipitin Tests
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Protein Binding / physiology
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Protein Structure, Tertiary
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TRPC Cation Channels
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Transient Receptor Potential Channels
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Yeasts / chemistry
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Yeasts / physiology
Substances
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Calcium Channels
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Calmodulin-Binding Proteins
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Drosophila Proteins
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Membrane Proteins
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TRPC Cation Channels
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Transient Receptor Potential Channels
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transient receptor potential cation channel, subfamily C, member 1
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trpl protein, Drosophila