Indentification and Analysis of Occludin Phosphosites: A Combined Mass Spectroscoy and Bioinformatics Approach

Journal Article · Thu Jan 01 00:00:00 EST 2009 · Journal of Proteome Research

DOI:https://doi.org/10.1021/pr7007913· OSTI ID:980266

Sundstrom, J; Tash, B; Murakami, T; Flanagan, J; Bewley, M; Stanley, B; Gonsar, K; Antonetti, D

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.

• Research Organization: Brookhaven National Lab. (BNL), Upton, NY (United States). National Synchrotron Light Source
• Sponsoring Organization: Doe - Office Of Science
• DOE Contract Number: DE-AC02-98CH10886
• OSTI ID: 980266
• Report Number(s): BNL-93184-2010-JA; TRN: US201015%%1651
• Journal Information: Journal of Proteome Research, Vol. 8
• Country of Publication: United States
• Language: English

Related Subjects

36 MATERIALS SCIENCE
CRYSTAL STRUCTURE
DATA ANALYSIS
IN VIVO
MEMBRANES
PHOSPHORYLATION
PROTEINS
SPECTROSCOPY
national synchrotron light source