Premium
A link between two tumorigenic proteins, CD44 and p21 WAF1 : CD44 increases phorbol ester‐induced expression of p21 WAF1 by stabilizing its mRNA and extending protein half‐life
Author(s) -
Lindner Christina,
Urbánek Pavel,
Pavelka Birgit,
Hartmann Monika,
Herrlich Peter
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.07.010
Subject(s) - radixin , cd44 , moesin , ezrin , protein kinase c , messenger rna , phorbol , microbiology and biotechnology , chemistry , protein kinase a , kinase , cell , biology , biochemistry , cytoskeleton , gene
The cell surface glycoprotein CD44 enhances phorbol‐12‐myristate 13‐acetate (TPA)‐induced expression of p21 WAF1 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.