2. Academic Validation
  3. Structural basis for the interaction between the Golgi reassembly-stacking protein GRASP65 and the Golgi matrix protein GM130

Structural basis for the interaction between the Golgi reassembly-stacking protein GRASP65 and the Golgi matrix protein GM130

  • J Biol Chem. 2015 Oct 30;290(44):26373-82. doi: 10.1074/jbc.M115.657940.
Fen Hu 1,  Xiaoli Shi 1,  Bowen Li 1,  Xiaochen Huang 1,  Xavier Morelli 2,  Ning Shi 3
Affiliations

Affiliations

  • 1 From the State Key Laboratory of Structural Chemistry, Fujian Institute of Research on the Structure of Matter, Chinese Academy of Sciences, Fuzhou 350002, China and.
  • 2 the CNRS UMR7258, INSERM U1068, Aix-Marseille Université UM105, Institut Paoli-Calmettes, Marseille F-13009, France.
  • 3 From the State Key Laboratory of Structural Chemistry, Fujian Institute of Research on the Structure of Matter, Chinese Academy of Sciences, Fuzhou 350002, China and shining@fjirsm.ac.cn ningshi2000@hotmail.com.
PMID: 26363069 DOI: 10.1074/jbc.M115.657940
Abstract

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.

Keywords

GM130, GRASP65, PDZ domain, Golgi stacking, vesicle tethering; Golgi; protein assembly; protein complex; protein-protein interaction; vesicles.

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