ABSTRACT
Integrins mediate the bidirectional transfer of signals across the plasma membrane. Clustering the chimeric receptors on the cell surface can activate signaling pathways by mechanisms similar to endogenous integrins. The chimeric receptors can be used to identify and analyze signaling events triggered by integrin β cytoplasmic domains. Chimeric receptors have been useful in defining a role for integra β cytoplasmic domains in triggering FAK phosphorylation, as well as in identifying amino acid motifs within p cytoplasmic domains required to activate FAK phosphorylation. Expression of high levels of chimeric receptors containing β cytoplasmic domains inhibit cell attachment. The chimeric receptors are thought to function as dominant inhibitors, either by sequestering cytoplasmic proteins required for endogenous integrin function or by activating signaling pathways that inhibit integrin function.
