Accordingly, reduction of MK2-mediated Hsp27 phosphorylation by reduced p38 kinase activity from suppression by Her2 in breast cancer cells contributes to β-catenin activation by allowing unphosphorylated Hsp27 to bind to β-catenin; this allows phosphorylation of β-catenin by Src, starting a chain of signaling that leads to dissemination phenotypes in early lesion breast cancer cells [123]. Here, ERBB2 is linked to breast cancer.