AI Article Synopsis
- INAD plays a crucial role in assembling essential enzymes for light signaling in compound eyes, but the interaction mechanism with NORPA, a key enzyme, remains unclear.
- Research reveals that the C-terminal coiled-coil domain and PDZ-binding motif of NORPA bind strongly and uniquely to INAD's PDZ45 tandem, which is vital for rapid light signal processing.
- The findings indicate that INADL may serve as a mammalian equivalent to INAD, with similar binding mechanisms to PLCβ4, suggesting a conserved evolutionary role for PDZ tandems in PLCβ signaling across different species.
Article Abstract
INAD assembles key enzymes of the 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 Cβ, PLCβ), 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 PLCβ4 with a mode that is strikingly similar to that of the INAD-NORPA complex, as revealed by the structure of the INADL PDZ89-PLCβ4 CC-PBM complex. Therefore, our study suggests that the highly specific PDZ tandem - PLCβ interactions are an evolutionarily conserved mechanism in PLCβ signaling in the animal kingdom.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6300352 | PMC |
| http://dx.doi.org/10.7554/eLife.41848 | DOI Listing |
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