FASEB J. 2010 Oct;24(10):4058-67. doi: 10.1096/fj.10-162925. Epub 2010 Jun 10.
Interaction between PKD1L3 and PKD2L1 through their transmembrane domains is required for localization of PKD2L1 at taste pores in taste cells of circumvallate and foliate papillae.
Ishimaru, Y., Katano, Y., Yamamoto, K., Akiba, M., Misaka, T., Roberts, R. W., Asakura, T., Matsunami, H., Abe, K.,
["Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan. ayishi@mail.ecc.u-tokyo.ac.jp"]
["Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan. ayishi@mail.ecc.u-tokyo.ac.jp"]
The polycystic kidney disease 1-like 3 (PKD1L3) and polycystic kidney disease 2-like 1 (PKD2L1) proteins have been proposed to form heteromers that function as sour taste receptors in mammals. Here, we show that PKD1L3 and PKD2L1 interact through their transmembrane domains, and not through the coiled-coil domain, by coimmunoprecipitation experiments using a series of deletion mutants. Deletion mutants lacking the critical interaction region were not transported to the cell surface and remained in the cytoplasm, whereas PKD1L3 and PKD2L1 proteins were expressed at the cell surface when both are transfected. Calcium imaging analysis revealed that neither the coiled-coil domain nor the EF-hand domain located in the C-terminal cytoplasmic tail of PKD2L1 was required for response on stimulation with an acidic solution. Finally, PKD2L1 did not localize to the taste pore but was distributed throughout the cytoplasm in taste cells of circumvallate and foliate papillae in PKD1L3(-/-) mice, whereas it localized to the taste pore in wild-type mice. Collectively, these results suggest that the interaction between PKD1L3 and PKD2L1 through their transmembrane domains is essential for proper trafficking of the channels to the cell surface in taste cells of circumvallate and foliate papillae and in cultured cells.
PMID: 20538909

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Validation: In vivo validation
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Assay with endogenous proteins | Assay with overexpressed proteins | Reference | ||||||||
Cell or tissue | Cell or tissue | TRP channel construct | Interactor construct | |||||||
TRP channel | Interactor | Method | Species | Region | Species | Region | ||||
TRPP2 |
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PKD1L3/Polycystin-1L3 | Co-immunoprecipitation | HEK293T | Mouse | Full-length | Mouse | Full-length | 20538909 |
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click the arrow icon to show interactions only between the corresponding TRP channel and the interactor)

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Characterization
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Binding region mapping | Stoichiometry | Affinity (Kd) | Reference | |||||||
TRP channel | Interactor | |||||||||
TRP channel | Interactor | Method | Species | Region | Species | Region | ||||
TRPP2 |
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PKD1L3/Polycystin-1L3 | Co-immunoprecipitation | Mouse | Not determined | Mouse | 1896-2040 | 20538909 |
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click the arrow icon to show interactions only between the corresponding TRP channel and the interactor)

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Functional consequence
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TRP channel | Interactor | Method | Post-translational modification | Subcellular trafficking | Activity | Reference | ||||||
TRPP2 |
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PKD1L3/Polycystin-1L3 | Co-immunofluorescence staining | Increase in plasma membrane level | 20538909 |
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click the arrow icon to show interactions only between the corresponding TRP channel and the interactor)
