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Structural domains required for channel function of the mouse transient receptor potential protein homologue TRP1beta

Item Type:Article
Title:Structural domains required for channel function of the mouse transient receptor potential protein homologue TRP1beta
Creators Name:Engelke, M. and Friedrich, O. and Budde, P. and Schaefer, C. and Niemann, U. and Zitt, C. and Juengling, E. and Rocks, O. and Lueckhoff, A. and Frey, J.
Abstract:Transient receptor potential proteins (TRP) are supposed to participate in the formation of store-operated Ca(2+) influx channels by co-assembly. However, little is known which domains facilitate the interaction of subunits. Contribution of the N-terminal coiled-coil domain and ankyrin-like repeats and the putative pore region of the mouse TRP1beta (mTRP1beta) variant to the formation of functional cation channels were analyzed following overexpression in HEK293 (human embryonic kidney) cells. MTRP1beta expressing cells exhibited enhanced Ca(2+) influx and enhanced whole-cell membrane currents compared to mTRP1beta deletion mutants. Using a yeast two-hybrid assay only the coiled-coil domain facilitated homodimerization of the N-terminus. These results suggest that the N-terminus of mTRP1beta is required for structural organization thus forming functional channels.
Keywords:Transient Receptor Potential Protein, Coiled-Coil Domain, Ankyrin-Like Repeat, HEK293 Cell, Patch Clamp, Yeast Two-Hybrid System, Animals, Mice
Source:FEBS Letters
ISSN:0014-5793
Publisher:Elsevier (The Netherlands)
Volume:523
Number:1-3
Page Range:193-199
Date:17 July 2002
Official Publication:https://doi.org/10.1016/S0014-5793(02)02971-X
PubMed:View item in PubMed

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