Structural highlights
Function
Q91UZ1_MOUSE The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes.[PIRNR:PIRNR000956]
Publication Abstract from PubMed
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 Cbeta, PLCbeta), 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 PLCbeta4 with a mode that is strikingly similar to that of the INAD-NORPA complex, as revealed by the structure of the INADL PDZ89-PLCbeta4 CC-PBM complex. Therefore, our study suggests that the highly specific PDZ tandem - PLCbeta interactions are an evolutionarily conserved mechanism in PLCbeta signaling in the animal kingdom.
An unexpected INAD PDZ tandem-mediated plcbeta binding in Drosophila photo receptors.,Ye F, Huang Y, Li J, Ma Y, Xie C, Liu Z, Deng X, Wan J, Xue T, Liu W, Zhang M Elife. 2018 Dec 10;7. pii: 41848. doi: 10.7554/eLife.41848. PMID:30526850[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ye F, Huang Y, Li J, Ma Y, Xie C, Liu Z, Deng X, Wan J, Xue T, Liu W, Zhang M. An unexpected INAD PDZ tandem-mediated plcbeta binding in Drosophila photo receptors. Elife. 2018 Dec 10;7. pii: 41848. doi: 10.7554/eLife.41848. PMID:30526850 doi:http://dx.doi.org/10.7554/eLife.41848
