Journal
EMBO JOURNAL
Volume 39, Issue 8, Pages -Publisher
WILEY
DOI: 10.15252/embj.2019104120
Keywords
Golgi; protein prenylation; PTAR1; SNARE; Ykt6
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Funding
- JSPS [16K08574, 17K15072, 16H05148]
- JST CREST [JPMJCR12M5]
- Takeda Science Foundation
- Grants-in-Aid for Scientific Research [16K08574, 16H05148, 17K15072] Funding Source: KAKEN
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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 beta 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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