An unexpected INAD PDZ tandem-mediated plcβ binding in <i>Drosophila</i> photo receptors.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 30526850.
- Also identified by DOI 10.7554/eLife.41848 and PMC identifier 6300352.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
INAD assembles key enzymes of the <i>Drosophila</i> 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.
Medical subject headings
- Drosophila Proteins
- Eye Proteins
- Phospholipase C beta
- Vision, Ocular