Structural domains required for channel function of the mouse transient receptor potential protein homologue TR1 beta
Engelke M, Friedrich O, Budde P, Schafer C, Niemann U, Zitt C, Jungling E, Rocks O, Luckhoff A, Frey J (2002)
FEBS LETTERS 523(1-3): 193-199.
Zeitschriftenaufsatz
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Autor*in
Engelke, M;
Friedrich, O;
Budde, P;
Schafer, C;
Niemann, U;
Zitt, C;
Jungling, E;
Rocks, O;
Luckhoff, A;
Frey, JürgenUniBi
Einrichtung
Abstract / Bemerkung
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.
Stichworte
transient receptor potential protein;
ankyrin-like;
repeat;
HEK293 cell;
yeast two-hybrid system;
patch clamp;
coiled-coil domain
Erscheinungsjahr
2002
Zeitschriftentitel
FEBS LETTERS
Band
523
Ausgabe
1-3
Seite(n)
193-199
ISSN
0014-5793
Page URI
https://pub.uni-bielefeld.de/record/1613977
Zitieren
Engelke M, Friedrich O, Budde P, et al. Structural domains required for channel function of the mouse transient receptor potential protein homologue TR1 beta. FEBS LETTERS. 2002;523(1-3):193-199.
Engelke, M., Friedrich, O., Budde, P., Schafer, C., Niemann, U., Zitt, C., Jungling, E., et al. (2002). Structural domains required for channel function of the mouse transient receptor potential protein homologue TR1 beta. FEBS LETTERS, 523(1-3), 193-199. https://doi.org/10.1016/S0014-5793(02)02971-X
Engelke, M, Friedrich, O, Budde, P, Schafer, C, Niemann, U, Zitt, C, Jungling, E, Rocks, O, Luckhoff, A, and Frey, Jürgen. 2002. “Structural domains required for channel function of the mouse transient receptor potential protein homologue TR1 beta”. FEBS LETTERS 523 (1-3): 193-199.
Engelke, M., Friedrich, O., Budde, P., Schafer, C., Niemann, U., Zitt, C., Jungling, E., Rocks, O., Luckhoff, A., and Frey, J. (2002). Structural domains required for channel function of the mouse transient receptor potential protein homologue TR1 beta. FEBS LETTERS 523, 193-199.
Engelke, M., et al., 2002. Structural domains required for channel function of the mouse transient receptor potential protein homologue TR1 beta. FEBS LETTERS, 523(1-3), p 193-199.
M. Engelke, et al., “Structural domains required for channel function of the mouse transient receptor potential protein homologue TR1 beta”, FEBS LETTERS, vol. 523, 2002, pp. 193-199.
Engelke, M., Friedrich, O., Budde, P., Schafer, C., Niemann, U., Zitt, C., Jungling, E., Rocks, O., Luckhoff, A., Frey, J.: Structural domains required for channel function of the mouse transient receptor potential protein homologue TR1 beta. FEBS LETTERS. 523, 193-199 (2002).
Engelke, M, Friedrich, O, Budde, P, Schafer, C, Niemann, U, Zitt, C, Jungling, E, Rocks, O, Luckhoff, A, and Frey, Jürgen. “Structural domains required for channel function of the mouse transient receptor potential protein homologue TR1 beta”. FEBS LETTERS 523.1-3 (2002): 193-199.
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