Department of Genomic Engineering, Research Institute of Genetic Engineering, Hankyong National University, 67 Seokjeong-dong, Anseong-si, Gyeonggi-do 456-749, Republic of Korea. sylee@hknu.ac.kr

The vanilloid receptor (VR1 or TRPV1) is a capsaicin (CAP)-sensitive non-selective cation channel. Although its channel activity is reportedly modulated through protein-protein interactions, to date very few VR1 interacting proteins have been identified. To address this issue, a yeast two-hybrid screening technique using the C-terminus of rVR1 as bait was employed. Upon interrogation of a mouse brain library, one gene product that interacts with VR1 and is highly homologous to human eferin was found. Its interaction with VR1 was confirmed by GST-pull-down and co-immunoprecipitation. When cotransfected into HEK cells, VR1 and eferin largely colocalize. Furthermore, in rat dorsal root ganglion cells, the rat eferin homologue also colocalizes with rVR1. However, this protein had no significant effect on VR1 channel activity in response to CAP. This was determined by two-electrode recording of oocytes and whole cell recording of HEK cells that were cotransfected with VR1 and human eferin.

Mesh Terms:
Amino Acid Sequence, Animals, Binding Sites, Carrier Proteins, Cell Line, Humans, Immunoprecipitation, Mice, Microscopy, Fluorescence, Molecular Sequence Data, Protein Binding, Receptors, Drug, Sequence Homology, Amino Acid

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