Download MendeleyA SNARE geranylgeranyltransferase essential for the organization of the Golgi apparatus.
Shirakawa, R., Goto-Ito, S., Goto, K., Wakayama, S., Kubo, H., Sakata, N., Trinh, D.A., Yamagata, A., Sato, Y., Masumoto, H., Cheng, J., Fujimoto, T., Fukai, S., Horiuchi, H.(2020) EMBO J 39: e104120-e104120
- PubMed: 32128853
- DOI: https://doi.org/10.15252/embj.2019104120
- Primary Citation of Related Structures:
6J6X, 6J74, 6J7F, 6J7X - PubMed Abstract:
Protein prenylation is essential for many cellular processes including signal transduction, cytoskeletal reorganization, and membrane trafficking. Here, we identify a novel type of protein prenyltransferase, which we named geranylgeranyltransferase type-III (GGTase-III). GGTase-III consists of prenyltransferase alpha subunit repeat containing 1 (PTAR1) and the β subunit of RabGGTase. Using a biotinylated geranylgeranyl analogue, we identified the Golgi SNARE protein Ykt6 as a substrate of GGTase-III. GGTase-III transfers a geranylgeranyl group to mono-farnesylated Ykt6, generating doubly prenylated Ykt6. The crystal structure of GGTase-III in complex with Ykt6 provides structural basis for Ykt6 double prenylation. In GGTase-III-deficient cells, Ykt6 remained in a singly prenylated form, and the Golgi SNARE complex assembly was severely impaired. Consequently, the Golgi apparatus was structurally disorganized, and intra-Golgi protein trafficking was delayed. Our findings reveal a fourth type of protein prenyltransferase that generates geranylgeranyl-farnesyl Ykt6. Double prenylation of Ykt6 is essential for the structural and functional organization of the Golgi apparatus.
Organizational Affiliation:
Department of Molecular and Cellular Biology, Institute of Development, Aging and Cancer, Tohoku University, Sendai, Japan.
