Structural domains required for channel function of the mouse transient receptor potential protein homologue TR1β

被引：37

作者：

Engelke, M

Friedrich, O

Budde, P

Schäfer, C

Niemann, U

Zitt, C

Jüngling, E

Rocks, O

Lückhoff, A

Frey, J

机构：

[1] Univ Bielefeld, Fak Chem, D-33615 Bielefeld, Germany

[2] Rhein Westfal TH Aachen, Inst Physiol, D-52074 Aachen, Germany

[3] Nordmark Arzneimittel GmbH & Co KG, D-25436 Uetersen, Germany

[4] BYK Gulden Lomberg GmbH, D-78467 Constance, Germany

[5] Max Planck Inst Mol Physiol, D-44227 Dortmund, Germany

来源：

FEBS LETTERS | 2002年 / 523卷 / 1-3期

关键词：

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

D O I：

10.1016/S0014-5793(02)02971-X

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：193 / 199

页数：7

共 36 条

[1] The use of the lipophilic fluorochrome CM-DiI for tracking the migration of lymphocytes [J].