An unexpected INAD PDZ tandem-mediated plc? binding in Drosophila photo receptors.

ABSTRACT: INAD assembles key enzymes of the Drosophila compound eye photo-transduction pathway into a supramolecular complex, supporting efficient and fast light signaling. However, the molecular mechanism that governs the interaction between INAD and NORPA (phospholipase C?, PLC?), a key step for the fast kinetics of the light signaling, is not known. Here, we show that the NORPA C-terminal coiled-coil domain and PDZ-binding motif (CC-PBM) synergistically bind to INAD PDZ45 tandem with an unexpected mode and unprecedented high affinity. Guided by the structure of the INAD-NORPA complex, we discover that INADL is probably a mammalian counterpart of INAD. The INADL PDZ89 tandem specifically binds to PLC?4 with a mode that is strikingly similar to that of the INAD-NORPA complex, as revealed by the structure of the INADL PDZ89-PLC?4 CC-PBM complex. Therefore, our study suggests that the highly specific PDZ tandem - PLC? interactions are an evolutionarily conserved mechanism in PLC? signaling in the animal kingdom.

SUBMITTER: Ye F 

PROVIDER: S-EPMC6300352 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature