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

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.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0014-0E3B-A Version Permalink: https://hdl.handle.net/11858/00-001M-0000-0014-0E3C-8
Genre: Journal Article
Alternative Title : FEBS Lett.

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 Creators:
Engelke, Michael, Author
Friedrich, Olaf, Author
Budde, Petra, Author
Schäfer, Christina, Author
Niemann, Ursula, Author
Zitt, Christof, Author
Jüngling, Eberhard, Author
Rocks, Oliver1, Author
Lückhoff, Andreas, Author
Frey, Jürgen, Author
Affiliations:
1Max Planck Institute of Molecular Physiology, Max Planck Society, ou_1753286              

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Free keywords: transient receptor potential protein; coiled-coil domain; ankyrin-like repeat; HEK293 cell; patch clamp; yeast two-hybrid system
 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.

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Language(s): eng - English
 Dates: 2002-07-17
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 15402
URI: http://dx.doi.org/10.1016/S0014-5793(02)02971-X
 Degree: -

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Title: FEBS Letters
  Alternative Title : FEBS Lett.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 523 (1-3) Sequence Number: 1 Start / End Page: 193 - 199 Identifier: -