Members of the ezrin–radixin–moesin (ERM) family of proteins are involved in multiple aspects of cell migration by acting both as crosslinkers between the membrane, receptors and the actin cytoskeleton, and as regulators of signalling molecules that are implicated in cell adhesion, cell polarity and migration. Increasing evidence suggests that the regulation of cell signalling and the cytoskeleton by ERM proteins is crucial during cancer progression. Thus, both their expression levels and subcellular localisation would affect tumour progression. High expression of ERM proteins has been shown in a variety of cancers. Mislocalisation of ERM proteins reduces the ability of cells to form cell–cell contacts and, therefore, promotes an invasive phenotype. Similarly, mislocalisation of ERM proteins impairs the formation of receptor complexes and alters the transmission of signals in response to growth factors, thereby facilitating tumour progression. In this Commentary, we address the structure, function and regulation of ERM proteins under normal physiological conditions as well as in cancer progression, with particular emphasis on cancers of epithelial origin, such as those from breast, lung and prostate. We also discuss any recent developments that have added to the understanding of the underlying molecular mechanisms and signalling pathways these proteins are involved in during cancer progression.

On page 268 of this article, the official name of NcK-interacting kinase (NIK) was incorrectly given as MAP3K14. The correct protein symbol is MAP4K4. The correct sentence should read: It has been proposed that the conserved threonine residues of these proteins can be phosphorylated in a tissue and cell-dependent manner through, for example, Rho-associated kinase (ROCK) (Hébert et al., 2008; Matsui et al., 1998), protein kinase Ca (PRKCA, hereafter referred to as PKCa) (Ng et al., 2001), NcK-interacting kinase (MAP4K4, hereafter referred to as NIK) (Baumgartner et al., 2006) lymphocyte-orientated kinase (STK10; hereafter referred to as LOK) (Belkina et al., 2009; Viswanatha et al., 2012) and others (see Table 1), which indicates that ERM proteins are involved in a wide variety of signalling pathways (Fig. 2). We apologise to the readers for any confusion that this error might have caused.

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