The interactions of the C-terminal region of the TRPC6 channel with calmodulin

被引：14

作者：

Friedlova, Eliska ^{[1
]}

Grycova, Lenka ^{[1
]}

Holakovska, Blanka ^{[1
]}

Silhan, Jan ^{[1
]}

Janouskova, Hana ^{[1
]}

Sulc, Miroslav ^{[2
,3
]}

Obsilova, Veronika ^{[1
]}

Obsil, Tomas ^{[1
,4
]}

Teisinger, Jan ^{[1
]}

机构：

[1] Acad Sci Czech Republic, Inst Physiol, CR-14220 Prague 4, Czech Republic

[2] Acad Sci Czech Republic, Inst Microbiol, CR-14220 Prague 4, Czech Republic

[3] Charles Univ Prague, Fac Sci, Dept Biochem, Prague 12843 2, Czech Republic

[4] Charles Univ Prague, Fac Sci, Dept Phys & Macromol Chem, Prague 12843 2, Czech Republic

来源：

NEUROCHEMISTRY INTERNATIONAL | 2010年 / 56卷 / 02期

关键词：

TRPC6; Calmodulin; Fluorescence anisotropy; BINDING; PROTEINS; RECEPTOR; DOMAIN; MODEL;

D O I：

10.1016/j.neuint.2009.11.009

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：

The transient receptor potential channel TRPC6 is a non-selective cation channel which modulates the calcium level in eukaryotic cells (including sensory receptor cells) in response to external signals. Calmodulin (CaM) is a ubiquitously expressed Ca2+ binding protein that is an important mediator of Ca2+-dependent regulation of the TRPC6 channel. One CaM binding site was identified within the C-tail of TRPC6. The aim of this study is to map in detail the CaM and inositol (1,4,5)-triphosphate receptor binding (CIRB) domain in the C-terminal region of mouse TRPC6 that is capable of interacting with CaM using in vitro binding assays. Besides the set of positively charged amino acid residues Arg852, Lys856, Arg864, Lys859/Arg860, a hydrophobic Ile857, at the position 1 in 1-5-10 motif, was located and the effect of replacing it with a neutral residue was tested using fluorescence anisotropy measurement. Participation of Ile857 could indicate a strong role of this conserved CaM binding motif. (C) 2009 Elsevier Ltd. All rights reserved.

引用

页码：363 / 366

页数：4

共 16 条

[1] Both the N-terminal loop and wing W2 of the forkhead domain of transcription factor FoxO4 are important for DNA binding [J].

Boura, Evzen ;

Silhan, Jan ;

Herman, Petr ;

Vecer, Jaroslav ;

Sulc, Miroslav ;

Teisinger, Jan ;

Obsilova, Veronika ;

Obsil, Tomas .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2007, 282 (11) :8265-8275

[2] The capsaicin receptor: a heat-activated ion channel in the pain pathway [J].

Caterina, MJ ;

Schumacher, MA ;

Tominaga, M ;

Rosen, TA ;

Levine, JD ;

Julius, D .

NATURE, 1997, 389 (6653) :816-824

[3] Coot:: model-building tools for molecular graphics [J].

Emsley, P ;

Cowtan, K .

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2004, 60 :2126-2132

[4] Ionic interactions are essential for TRPV1 C-terminus binding to calmodulin [J].

Grycova, Lenka ;

Lansky, Zdenek ;

Friedlova, Eliska ;

Obsilova, Veronika ;

Janouskova, Hana ;

Obsil, Tomas ;

Teisinger, Jan .

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2008, 375 (04) :680-683

[5] SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling [J].

Guex, N ;

Peitsch, MC .

ELECTROPHORESIS, 1997, 18 (15) :2714-2723

[6] Integration of phosphoinositide- and calmodulin-mediated regulation of TRPC6 [J].

Kwon, Young ;

Hofmann, Thomas ;

Montell, Craig .

MOLECULAR CELL, 2007, 25 (04) :491-503

[7]

Lakowicz J.R., 2006, Principles of Fluorescence Spectroscopy, V3rd, DOI DOI 10.1007/978-0-387-46312-4

[8] Ca2+/calmodulin binds to and modulates P/Q-type calcium channels [J].

Lee, A ;

Wong, ST ;

Gallagher, D ;

Li, B ;

Storm, DR ;

Scheuer, T ;

Catterall, WA .

NATURE, 1999, 399 (6732) :155-159

[9] Sequence motifs for calmodulin recognition [J].

Rhoads, AR ;

Friedberg, F .

FASEB JOURNAL, 1997, 11 (05) :331-340

[10] Single-step affinity purification of recombinant proteins using a self-excising module from Neisseria meningitidis FrpC [J].

Sadilkova, Lenka ;

Osicka, Radim ;

Sulc, Miroslav ;

Linhartova, Irena ;

Novak, Petr ;

Sebo, Peter .

PROTEIN SCIENCE, 2008, 17 (10) :1834-1843

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