Journal
JOURNAL OF PROTEOME RESEARCH
Volume 8, Issue 2, Pages 808-817Publisher
AMER CHEMICAL SOC
DOI: 10.1021/pr7007913
Keywords
tight junction; occludin; phosphorylation; VEGF; phosphosite mapping
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Funding
- NEI NIH HHS [R01 EY012021, EY012021, R01 EY012021-09] Funding Source: Medline
- NIGMS NIH HHS [R01 GM094526] Funding Source: Medline
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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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