Faculty Advisor

Adams, David S.

Abstract

Previous studies have shown that tyrosine phosphorylation states of adherens junction proteins of endothelial cells are sensitive to membrane cholesterol levels (Corvera et al, 2000). Consequently, endothelial membranes were analyzed by using low concentrations, 0.01%, of a membrane-permeable cholesterol-sequestering agent, digitonin, to identify proteins responsible for the dephosphorylation activity. One such protein, SHP2 tyrosine phosphatase, was identified in membranes extracted with digitonin. Although SHP2 is known to associate with adherens junction proteins in a manner dependent on phosphorylated tyrosines and SH2 domains, this study suggests a new mode of SHP2 binding dependent on cholesterol.

Publisher

Worcester Polytechnic Institute

Date Accepted

January 2002

Major

Biotechnology

Project Type

Major Qualifying Project

Accessibility

Restricted-WPI community only

Advisor Department

Biology and Biotechnology

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