RGA protein associates with a TRPV ion channel during biosynthesis and trafficking

TRPV ion channels transduce a range of temperature stimuli. We proposed that analysis of the protein–protein interactions made by TRPV2 might give insight into the key issues surrounding this channel. These issues include the potential functional significance of TRPV2 in non‐sensory tissues, the mol...

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Bibliographic Details
Published in:Journal of cellular biochemistry 2004-03, Vol.91 (4), p.808-820
Main Authors: Barnhill, Jason C., Stokes, Alexander J., Koblan-Huberson, Murielle, Shimoda, Lori M.N., Muraguchi, Atsushi, Adra, Chaker N., Turner, Helen
Format: Article
Language:English
Subjects:
Animals
calcium channels
Cell Line
Cell Membrane - metabolism
Cytoplasm - metabolism
heat
Humans
Immunoprecipitation
Ion Channels - genetics
Ion Channels - metabolism
mast cells
Membrane Proteins - biosynthesis
Membrane Proteins - chemistry
Membrane Proteins - genetics
Membrane Proteins - metabolism
Mice
Microscopy, Fluorescence
Molecular Sequence Data
MS4
Phylogeny
Protein Binding - drug effects
Protein Transport
Rats
Receptors, Drug - genetics
Receptors, Drug - metabolism
RNA, Messenger - genetics
RNA, Messenger - metabolism
Sequence Analysis, Protein
TRPV Cation Channels
Tunicamycin - pharmacology
Two-Hybrid System Techniques
vanilloid
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Summary:TRPV ion channels transduce a range of temperature stimuli. We proposed that analysis of the protein–protein interactions made by TRPV2 might give insight into the key issues surrounding this channel. These issues include the potential functional significance of TRPV2 in non‐sensory tissues, the molecules involved in transducing its activation signal(s) and the mechanism by which its trafficking to the cell surface is regulated. Here we describe the interaction of TRPV2 channel with the RGA gene product. RGA is a four‐transmembrane domain, intracellularly localized protein. RGA associates with TRPV2 in a rat mast cell line that is a native context for both proteins. The interaction between TRPV2 and RGA is transient and occurs intracellularly. RGA does not accompany TRPV2 to the cell surface. Formation of the TRPV2/RGA complex is dependent upon a cellular glycosylation event, suggesting that RGA may play a chaperone or targeting role for TRPV2 during the maturation of the ion channel protein. These data record a novel protein–protein interaction for TRPV2 and provide a foundation for future study of the potential regulatory contribution of RGA to TRPV2 function. © 2004 Wiley‐Liss, Inc.
ISSN:0730-2312
1097-4644
DOI:10.1002/jcb.10775