细丝蛋白C：缺氧期间KCNE2相互作用组的一种新成分。
Filamin C: a novel component of the KCNE2 interactome during hypoxia.
作者信息
Neethling Annika, Mouton Jomien, Loos Ben, Corfield Valerie, de Villiers Carin, Kinnear Craig
机构信息
DST/NRF Centre of Excellence in Biomedical Tuberculosis Research, SA MRC Centre for Tuberculosis Research, Division of Molecular Biology and Human Genetics, Department of Biomedical Sciences, Faculty of Medicine and Health Sciences, Stellenbosch University, South Africa.
Department of Physiological Sciences, Faculty of Science, Stellenbosch University, Stellenbosch, South Africa.
出版信息
Cardiovasc J Afr. 2016 Jan-Feb;27(1):4-11. doi: 10.5830/CVJA-2015-049.
AIM
KCNE2 encodes for the potassium voltage-gated channel, KCNE2. Mutations in KCNE2 have been associated with long-QT syndrome (LQTS). While KCNE2 has been extensively studied, the functions of its C-terminal domain remain inadequately described. Here, we aimed to elucidate the functions of this domain by identifying its protein interactors using yeast two-hybrid analysis.
METHODS
The C-terminal domain of KCNE2 was used as bait to screen a human cardiac cDNA library for putative interacting proteins. Co-localisation and co-immunoprecipitation analyses were used for verification.
RESULTS
Filamin C (FLNC) was identified as a putative interactor with KCNE2. FLNC and KCNE2 co-localised within the cell, however, a physical interaction was only observed under hypoxic conditions.
CONCLUSION
The identification of FLNC as a novel KCNE2 ligand not only enhances current understanding of ion channel function and regulation, but also provides valuable information about possible pathways likely to be involved in LQTS pathogenesis.
目的
KCNE2编码钾离子电压门控通道KCNE2。KCNE2中的突变与长QT综合征（LQTS）相关。虽然KCNE2已被广泛研究，但其C末端结构域的功能仍描述不足。在此，我们旨在通过酵母双杂交分析鉴定其蛋白质相互作用因子来阐明该结构域的功能。
方法
将KCNE2的C末端结构域用作诱饵，筛选人心脏cDNA文库以寻找假定的相互作用蛋白。采用共定位和免疫共沉淀分析进行验证。
结果
细丝蛋白C（FLNC）被鉴定为与KCNE2的假定相互作用因子。FLNC和KCNE2在细胞内共定位，然而，仅在缺氧条件下观察到物理相互作用。
结论
FLNC作为一种新型KCNE2配体的鉴定不仅增强了当前对离子通道功能和调节的理解，还提供了关于可能参与LQTS发病机制的途径的有价值信息。
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