A SNARE geranylgeranyltransferase essential for the organization of the Golgi apparatus

Ryutaro Shirakawa, Sakurako Goto-Ito, Kota Goto, Shonosuke Wakayama, Haremaru Kubo, Natsumi Sakata, Duc Anh Trinh, Atsushi Yamagata, Yusuke Sato, Hiroshi Masumoto, Jinglei Cheng, Toyoshi Fujimoto, Shuya Fukai, Hisanori Horiuchi

研究成果: Article査読

13 被引用数 (Scopus)


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.

ジャーナルEMBO Journal
出版ステータスPublished - 2020 4 15

ASJC Scopus subject areas

  • 神経科学(全般)
  • 分子生物学
  • 生化学、遺伝学、分子生物学(全般)
  • 免疫学および微生物学(全般)


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