期刊
JOURNAL OF PROTEOME RESEARCH
卷 8, 期 2, 页码 808-817出版社
AMER CHEMICAL SOC
DOI: 10.1021/pr7007913
关键词
tight junction; occludin; phosphorylation; VEGF; phosphosite mapping
资金
- NEI NIH HHS [R01 EY012021, EY012021, R01 EY012021-09] Funding Source: Medline
- NIGMS NIH HHS [R01 GM094526] Funding Source: Medline
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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