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

Jeffrey M. Sundstrom, Brian R. Tash, Tomoaki Murakami, John M. Flanagan, Maria C. Bewley, Bruce A. Stanley, Kristin B. Gonsar, David A. Antonetti

Research output: Contribution to journalArticlepeer-review

47 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)808-817
Number of pages10
JournalJournal of Proteome Research
Volume8
Issue number2
DOIs
StatePublished - Feb 2009

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Chemistry(all)

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