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Integrins are receptors for extracellular matrix proteins that engage in reciprocal crosstalk with growth factor receptors. Recent work identifies a unique mechanism for the regulation of growth factor receptor phosphorylation by integrins, indicating multiple ways of achieving cooperation between these major signalling systems.
Small GTPases of the Rab family are essential for the control of membrane transport between intracellular compartments. Recent work has shown that on melanosome membranes, Rab27a initiates the formation of a receptor complex that allows the recruitment of the actin-based motor myosin Va. This study provides a molecular basis for several pathologies that result in pigmentation defects in both mouse and humans.
Multicellular organisms must coordinate signals from adhesion receptors with those from other signalling receptors (for example, growth factor receptors). Here, we briefly review paradigms of integrin–adhesion-receptor signalling. We discuss how adhesive signalling is coordinately regulated through intersecting networks. We also examine some examples of how some forms of integrin crosstalk may lead to unforeseen and potentially deleterious responses.