Identification and analysis of occludin phosphosites: a combined mass spectrometry and bioinformatics approach.

Identification and analysis of occludin phosphosites: a combined mass spectrometry and bioinformatics approach.
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DOI:
10.1021/pr7007913
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发表时间:
2009-02
影响因子:
4.4
通讯作者:
Antonetti, David A.
Antonetti, David A.
中科院分区:
生物学2区
文献类型:
--
作者:
Sundstrom, Jeffrey M.;Tash, Brian R.;Murakami, Tomoaki;Flanagan, John M.;Bewley, Maria C.;Stanley, Bruce A.;Gonsar, Kristin B.;Antonetti, David A.

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闭合蛋白是紧密连接的一个膜组成部分,其分子功能尚不清楚。结合MS数据分析和生物信息学,VEGF诱导的磷酸化位点定位在occludin。Ser 490的体内磷酸化得到验证,结合晶体结构分析的蛋白质相互作用研究表明,Ser 490磷酸化减弱了occludin和ZO-1之间的相互作用。这项研究表明,结合MS数据和生物信息学可以成功地确定新的磷酸化位点从有限的样品。
The molecular function of occludin, an integral membrane component of tight junctions, remains unclear. VEGF-induced phosphorylation sites were mapped on occludin by combining MS data analysis with bioinformatics. In vivo phosphorylation of Ser490 was validated and protein interaction studies combined with crystal structure analysis suggest that Ser490 phosphorylation attenuates the interaction between occludin and ZO-1. This study demonstrates that combining MS data and bioinformatics can successfully identify novel phosphorylation sites from limiting samples.
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