| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10871204 | FEBS Letters | 2013 | 7 Pages |
Abstract
The cell surface glycoprotein CD44 enhances phorbol-12-myristate 13-acetate (TPA)-induced expression of p21WAF1 by stabilizing its mRNA and enhancing the protein's half-life in several cell lines. Only the plasma membrane-anchored cytoplasmic tail of CD44 and its interacting ezrin, radixin, moesin (ERM) proteins are required for this effect. A mitogen activated kinase (MEK) inhibitor abolishes the action of CD44 on p21. Down-regulation of p21 dramatically decreased anchorage-independence of a cancer cell line, whereas CD44 expression in this background could partially rescue the phenotype.
Keywords
phorbol-12-myristate 13-acetateP21PKCCHXezrinERMΔEqRT-PCRCD44tPACTRLezrin, radixin, moesinFACSMAPKempty vectorintracellular domainICDcycloheximidefluorescence activated cell sortingMEKmitogen activated kinaseKnockdownquantitative real-time PCRERM proteinsProtein kinase Cmitogen activated protein kinaseControl
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Authors
Christina Lindner, Pavel Urbánek, Birgit Pavelka, Monika Hartmann, Peter Herrlich,