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Cell adhesion molecules, such as integrins, cadherins, the immunoglobulin superfamily of cell adhesion molecules and selectins, play important structural roles and are involved in various signal transduction processes. As an initial step in the infectious process, many bacterial pathogens adhere to cell adhesion molecules as a means of exploiting the underlying signaling pathways, entering into host cells or establishing extracellular persistence. Often, bacteria are able to bind to cell adhesion molecules by mimicking or acting in place of host cell receptors or their ligands. Recent studies have contributed to our understanding of bacterial adherence mechanisms and the consequences of receptor engagement; they have also highlighted alternative functions of cell adhesion molecules. [Copyright &y& Elsevier]

Adhesion molecules, although catalytically inactive, are able to translate environmental cues into complex intracellular signals. They can do this by associating with tyrosine kinase receptors for growth factors, which can prime, integrate or feedback adhesion-based signals. Recent results show that reciprocal crosstalk between the two systems is only one facet of such a collaboration, and that unconventional and alternative hierarchies can be established in which, on the one hand, cell adhesion can trigger ligand-independent activation of growth factor receptors, and, on the other, growth factors can induce adhesion molecules to propagate adhesion-independent signals. [Copyright &y& Elsevier]