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The crystal structure of the FERM and C-terminal domain complex of Drosophila Merlin by Fayou Zhang; Beibei Liu; Yaqi Gao; Jiafu Long; Hao Zhou is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is The crystal structure of the FERM and C-terminal domain complex of Drosophila Merlin about?

NF2/Merlin is an upstream regulator of hippo pathway, and it has two states: an auto-inhibited "closed" state and an active "open" form. Previous studies showed that Drosophila Merlin adopts a more closed conformation. However, the molecular mechanism of conformational regulation remains poorly understood. Here, we first confirmed the strong interaction between FERM and the C-terminal domain (CTD) of Merlin, and then determined the crystal structure of the FERM/CTD complex, which reveals the structural basis of Merlin adopting a more closed conformation compared to its human cognate NF2. Interestingly, we found that the conserved lipid-binding site of Merlin might be masked by a linker. Confocal analyses confirmed that all putative lipid-binding site are very important for the membranal location of Merlin. More, we found that the phosphomimic Thr616Asp mutation weakens the interaction between FERM and CTD of Merlin. Collectively, the crystal structure of the FERM/CTD complex not only provides a mechanistic explanation of functionally dormant conformation of Merlin may also serve as a foundation for revealing the mechanism of conformational regulation of Merlin.

Who reads The crystal structure of the FERM and C-terminal domain complex of Drosophila Merlin?

Author

Fayou Zhang; Beibei Liu; Yaqi Gao; Jiafu Long; Hao Zhou

Publisher

Elsevier BV

Published

2021

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)