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All rights reserved. http://resource.belframework.org/belframework/1.0/knowledge/large_corpus.bel http://purl.org/dc/elements/1.1/title BEL Framework Large Corpus Document http://resource.belframework.org/belframework/1.0/knowledge/large_corpus.bel http://purl.org/pav/authoredBy http://www.tkuhn.ch/bel2nanopub/RAaVw7JHsDOo_gu3qbHK91s-sCVtL4GgyWvbnfPqqEl4Y#_6 http://resource.belframework.org/belframework/1.0/knowledge/large_corpus.bel http://purl.org/pav/version 1.4 http://www.tkuhn.ch/bel2nanopub/RAaVw7JHsDOo_gu3qbHK91s-sCVtL4GgyWvbnfPqqEl4Y#_5 http://www.w3.org/ns/prov#value A second proposal has been that phosphorylation activates binding functions of moesin. In human platelets, for instance, thrombin activation leads to a rapid, but transient, increase in the phosphorylation of a single threonine, Thr558...This residue is conserved in moesin, ezrin, and radixin, and it is modified also in RAW macrophages (34), Swiss3T3 cells (29),1 NIH3T3 cells,2 and RB2H3 mast cells. Phosphorylation at this site is regulated by the activity of Rho, and Rho-associated kinase phosphorylates two residues in the C-terminal region, one of which is Thr558 (29). 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