Potential sites of CFTR activation by tyrosine kinases

IF 3.3 3区 生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY
A. Billet, Yanlin Jia, T. Jensen, Yue‐xian Hou, X. Chang, J. Riordan, J. Hanrahan
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引用次数: 14

Abstract

ABSTRACT The CFTR chloride channel is tightly regulated by phosphorylation at multiple serine residues. Recently it has been proposed that its activity is also regulated by tyrosine kinases, however the tyrosine phosphorylation sites remain to be identified. In this study we examined 2 candidate tyrosine residues near the boundary between the first nucleotide binding domain and the R domain, a region which is important for channel function but devoid of PKA consensus sequences. Mutating tyrosines at positions 625 and 627 dramatically reduced responses to Src or Pyk2 without altering the activation by PKA, suggesting they may contribute to CFTR regulation.
酪氨酸激酶激活CFTR的潜在位点
CFTR氯通道受到多个丝氨酸残基磷酸化的严格调控。最近有人提出,其活性也受酪氨酸激酶的调节,但酪氨酸磷酸化位点仍有待确定。在这项研究中,我们在第一核苷酸结合域和R结构域之间的边界附近检测了2个候选酪氨酸残基,该区域对通道功能很重要,但缺乏PKA一致序列。位置625和627的酪氨酸突变显著降低了对Src或Pyk2的反应,而不改变PKA的激活,这表明它们可能有助于CFTR调控。
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来源期刊
Channels
Channels 生物-生化与分子生物学
CiteScore
5.90
自引率
0.00%
发文量
21
审稿时长
6-12 weeks
期刊介绍: Channels is an open access journal for all aspects of ion channel research. The journal publishes high quality papers that shed new light on ion channel and ion transporter/exchanger function, structure, biophysics, pharmacology, and regulation in health and disease. Channels welcomes interdisciplinary approaches that address ion channel physiology in areas such as neuroscience, cardiovascular sciences, cancer research, endocrinology, and gastroenterology. Our aim is to foster communication among the ion channel and transporter communities and facilitate the advancement of the field.
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