Structural domains required for channel function of the mouse transient 
receptor potential protein homologue TRP1β

Engelke, Michael; Friedrich, Olaf; Budde, Petra; Schäfer, Christina; Niemann, Ursula; Zitt, Christof; Jüngling, Eberhard; Rocks, Oliver; Lückhoff, Andreas; Frey, Jürgen

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Structural domains required for channel function of the mouse transient receptor potential protein homologue TRP1β

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Rocks, Oliver
Max Planck Institute of Molecular Physiology, Max Planck Society;

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Citation

Engelke, M., Friedrich, O., Budde, P., Schäfer, C., Niemann, U., Zitt, C., et al. (2002). Structural domains required for channel function of the mouse transient receptor potential protein homologue TRP1β. FEBS Letters, 523(1-3): 1, pp. 193-199. Retrieved from http://dx.doi.org/10.1016/S0014-5793(02)02971-X.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0014-0E3B-A

Abstract

Transient receptor potential proteins (TRP) are supposed to participate in the formation of store-operated Ca2+ 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 Ca2+ 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. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.