Interaction of Sedlin with chloride intracellular channel proteins

FEBS Letters

Fan, Libin¹  Yu, Wei¹  Zhu, Xueliang¹ 

[1] Laboratory of Molecular Cell Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, 320 Yue Yang Road, Shanghai 200031, PR China

关键词: CLIC1;    Sedlin;    TRAPP complex;    Interaction;    AD;    Gal4 activation domain;    BD;    Gal4 DNA-binding domain;    CLIC;    chloride intracellular channel protein;    ER;    endoplasmic reticulum;    ERGIC;    ER-to-Golgi intermediate compartment;    β-gal;    β-galactosidase;    GFP;    green fluorescence protein;    TRAPP;    transport protein particle;   

DOI  :  10.1016/S0014-5793(03)00228-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Sedlin is an evolutionarily conserved protein encoded by the causative gene SEDL for spondyloepiphyseal dysplasia tarda. Nevertheless, how Sedlin mutations cause the disease remains unknown. Here, the intracellular chloride channel protein CLIC1 was shown to associate with Sedlin by yeast two-hybrid screening. Green fluorescence protein-CLIC1 readily co-immunoprecipitated with FLAG-Sedlin. In addition, both proteins colocalized extensively in cytoplasmic vesicular/reticular structures in COS-7 cells, suggesting their interaction at intracellular membranous organelles. Sedlin also associated with CLIC2 in yeast two-hybrid assays. The link between Sedlin and the intracellular chloride channels is the first step to understand their functional interplays.

【 授权许可】

Unknown