Schematic to summarize DGK-α’s role in RCP-dependent events. Inhibition of αvβ3 or expression of mutant p53273H promotes recruitment of RCP to endosomal α5β1. Association of α5β1 with RCP is not a DGK-dependent event and does not require RCP’s PA-binding C2 domain. RCP/integrin recycling vesicles can then move up and down the pseudopod shaft, and the role of DGK-α is to generate PA species that enable the tethering of RCP at pseudopod tips, an event that requires RCP’s C2 domain. Of the lipid species detected in the mass spectrometric analysis, inhibition or silencing of DGK-α most significantly affects the interconversion of 38:4 DAG to 38:4 PA. The 38:4 species of PA is therefore depicted as the most likely to be involved in tethering RCP at pseudopod tips.
