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An unexpected INAD PDZ tandem-mediated PLCβ binding in Drosophila photo receptors.
ELife 2018 December 11
INAD assembles key enzymes of Drosophila compound eye photo-transduction pathway into a supramolecular complex, supporting efficient and fast light signaling. However, the molecular mechanism governing 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 unprecedentedly high affinity. Guided by the INAD/NORPA complex structure, we discover that INADL is likely a mammalian counterpart of INAD. The INADL PDZ89 tandem specifically binds to PLCβ4 with a strikingly similar mode 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 of the animal kingdom.
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