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A SNARE geranylgeranyltransferase essential for the organization of the Golgi apparatus
Author(s) -
Shirakawa Ryutaro,
GotoIto Sakurako,
Goto Kota,
Wakayama Shonosuke,
Kubo Haremaru,
Sakata Natsumi,
Trinh Duc Anh,
Yamagata Atsushi,
Sato Yusuke,
Masumoto Hiroshi,
Cheng Jinglei,
Fujimoto Toyoshi,
Fukai Shuya,
Horiuchi Hisanori
Publication year - 2020
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.15252/embj.2019104120
Subject(s) - library science , sendai virus , biology , computer science , genetics , gene
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 ( GGT ase‐ III ). GGT ase‐ III consists of prenyltransferase alpha subunit repeat containing 1 ( PTAR 1) and the β subunit of Rab GGT ase. Using a biotinylated geranylgeranyl analogue, we identified the Golgi SNARE protein Ykt6 as a substrate of GGT ase‐ III . GGT ase‐ III transfers a geranylgeranyl group to mono‐farnesylated Ykt6, generating doubly prenylated Ykt6. The crystal structure of GGT ase‐ III in complex with Ykt6 provides structural basis for Ykt6 double prenylation. In GGT ase‐ 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.