Functional dissection of the R domain of cystic fibrosis transmembrane conductance regulator 1

FEBS Letters

Tasch, Jason E.¹  Zhao, Jiying²  Ma, Jianjie²  Zerhusen, Bryan²  Davis, Pamela B.³ 

[1] Department of Molecular Biology and Microbiology, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA;Department of Physiology and Biophysics, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA;Department of Pediatrics, Case Western Reserve University School of Medicine, 10900 Euclid Ave., Cleveland, OH 44106, USA

关键词: Cystic fibrosis;    CFTR;    R domain;    Channel regulation;    CFTR;    cystic fibrosis transmembrane conductance regulator;    wt;    wild-type;    PCR;    polymerase chain reaction;    R domain;    regulatory domain;    PKA;    protein kinase A;    PKI;    protein kinase inhibitor;    PKC;    protein kinase C;    ABC;    ATP binding cassette;    RDP;    R domain protein;    PAGE;    polyacrylamide gel electrophoresis;    pS;    picosiemen;    fA;    femtoamperes;    SPQ;    6-methoxy-N-(3-sulfopropyl) quinolinium;    DPC;    diphenylcarboxylate;    aa;    amino acids;    NEM;    N-ethylmaleimide;   

DOI  :  10.1016/S0014-5793(99)00086-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Exogenously expressed unphosphorylated sub-domains of the R domain block CFTR Cl⁻ channels in the planar lipid bilayer, though the block differs from block with full length R domain. Full length R domain peptide (aa 588–855) blocks CFTR Cl⁻ channels quickly, completely and permanently [1]. Two sub-domains, RD1RD2 (aa 588–805) and RD2TM (aa 672–855), also inhibit CFTR Cl⁻ channels, but the block takes longer to effect and is not complete. Shorter sequences, RD1 (aa 588–746) and RD2 (aa 672–805), fail to effect any block. These data suggest that either the amino-terminal or carboxy-terminal portions of the R domain protein or its stabilized secondary structure are critical to functional regulation.

【 授权许可】

Unknown