A SNARE geranylgeranyltransferase essential for the organization of the Golgi apparatus.

The EMBO Journal
Ryutaro ShirakawaHisanori Horiuchi

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.

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Citations

Mar 24, 2020·The EMBO Journal·Amy F Roth, Nicholas G Davis
Oct 10, 2020·Journal of Biochemistry·Natsumi SakataHisanori Horiuchi
Nov 20, 2020·Biomolecules·Pradhipa Karuna MJulia Christina Gross
Jan 6, 2021·International Journal of Molecular Sciences·Ramesh KumarSujatha Sunil
Nov 23, 2020·Current Opinion in Chemical Biology·Ana Losada de la LastraEdward W Tate
Mar 17, 2021·Proceedings of the National Academy of Sciences of the United States of America·Kaitlyn McGrathGabriela Caraveo
Apr 7, 2021·Chemical Reviews·Kiall F SuazoMark D Distefano
Jul 9, 2021·Journal of Medicinal Chemistry·Edyta Gendaszewska-DarmachKatarzyna M Błażewska

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