Faculty Opinions recommendation of Structural basis for the interaction between the Golgi reassembly-stacking protein GRASP65 and the Golgi matrix protein GM130.
Year: 2017
Type: peer-review
Abstract: Background: GRASP65 and GM130 play a key role in Golgi stacking. Results:The crystal structure of the GRASP65-GM130 complex reveals an unexpected binding mode.Conclusion: Both PDZ domains of GRASP65 interact with GM130.A novel mechanism for Golgi stacking is proposed.Significance: A novel interaction mode permits us to propose a new molecular basis for Golgi structure.GM130 and GRASP65 are Golgi peripheral membrane proteins that play a key role in Golgi stacking and vesicle tethering.However, the molecular details of their interaction and their structural role as a functional unit remain unclear.Here, we present the crystal structure of the PDZ domains of GRASP65 in complex with the GM130 C-terminal peptide at 1.96-Å resolution.In contrast to previous findings proposing that GM130 interacts with GRASP65 at the PDZ2 domain only, our crystal structure of the complex indicates that GM130 binds to GRASP65 at two distinct sites concurrently and that both the PDZ1 and PDZ2 domains of GRASP65 participate in this molecular interaction.Mutagenesis experiments support these structural observations and demonstrate that they are required for GRASP65-GM130 association.
Authors: Yanzhuang Wang, Shijiao Huang
Language: English
Subfield: Cell Biology
Domain: Life Sciences
Open Access status: green
OpenAlex ID: W4245954389