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

eLife | 2018

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 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.

Pubmed ID: 30526850 RIS Download

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This is a list of tools and resources that we have found mentioned in this publication.


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RRID:SCR_007255

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RRID:SCR_014224

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RRID:SCR_007255

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View all literature mentions

PyMOL (software resource)

RRID:SCR_000305

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View all literature mentions

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RRID:SCR_002815

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GraphPad Prism (software resource)

RRID:SCR_002798

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RRID:AB_627695

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Anti-Mouse IgG (whole molecule)-Peroxidase antibody produced in goat (antibody)

RRID:AB_258167

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View all literature mentions

HEK293T (cell line)

RRID:CVCL_0063

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View all literature mentions