| Autor: |
Fei Ye, Yuxin Huang, Jianchao Li, Yuqian Ma, Chensu Xie, Zexu Liu, Xiaoying Deng, Jun Wan, Tian Xue, Wei Liu, Mingjie Zhang |
| Jazyk: |
angličtina |
| Rok vydání: |
2018 |
| Předmět: |
|
| Zdroj: |
eLife, Vol 7 (2018) |
| Druh dokumentu: |
article |
| ISSN: |
2050-084X |
| DOI: |
10.7554/eLife.41848 |
| Popis: |
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. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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