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

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.

SUBMITTER: Sundstrom JM

PROVIDER: S-EPMC3677543 | biostudies-literature | 2009 Feb

REPOSITORIES: biostudies-literature

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

Sundstrom Jeffrey M JM Tash Brian R BR Murakami Tomoaki T Flanagan John M JM Bewley Maria C MC Stanley Bruce A BA Gonsar Kristin B KB Antonetti David A DA

Journal of proteome research 20090201 2

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 succe ...[more]

PMID: 19125584

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