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Tytuł pozycji:

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

Tytuł:
A SNARE geranylgeranyltransferase essential for the organization of the Golgi apparatus.
Autorzy:
Shirakawa R; Department of Molecular and Cellular Biology, Institute of Development, Aging and Cancer, Tohoku University, Sendai, Japan.
Goto-Ito S; Institute for Quantitative Biosciences, The University of Tokyo, Tokyo, Japan.; Synchrotron Radiation Research Organization, The University of Tokyo, Tokyo, Japan.
Goto K; Department of Molecular and Cellular Biology, Institute of Development, Aging and Cancer, Tohoku University, Sendai, Japan.
Wakayama S; Department of Molecular and Cellular Biology, Institute of Development, Aging and Cancer, Tohoku University, Sendai, Japan.
Kubo H; Department of Molecular and Cellular Biology, Institute of Development, Aging and Cancer, Tohoku University, Sendai, Japan.
Sakata N; Department of Molecular and Cellular Biology, Institute of Development, Aging and Cancer, Tohoku University, Sendai, Japan.
Trinh DA; Department of Molecular and Cellular Biology, Institute of Development, Aging and Cancer, Tohoku University, Sendai, Japan.
Yamagata A; Institute for Quantitative Biosciences, The University of Tokyo, Tokyo, Japan.; Synchrotron Radiation Research Organization, The University of Tokyo, Tokyo, Japan.
Sato Y; Institute for Quantitative Biosciences, The University of Tokyo, Tokyo, Japan.; Synchrotron Radiation Research Organization, The University of Tokyo, Tokyo, Japan.
Masumoto H; Biomedical Research Support Center, Nagasaki University School of Medicine, Nagasaki, Japan.
Cheng J; Department of Anatomy and Molecular Cell Biology, Nagoya University Graduate School of Medicine, Nagoya, Japan.
Fujimoto T; Research Institute for Diseases of Old Age, Juntendo University Graduate School of Medicine, Tokyo, Japan.
Fukai S; Institute for Quantitative Biosciences, The University of Tokyo, Tokyo, Japan.; Synchrotron Radiation Research Organization, The University of Tokyo, Tokyo, Japan.
Horiuchi H; Department of Molecular and Cellular Biology, Institute of Development, Aging and Cancer, Tohoku University, Sendai, Japan.
Źródło:
The EMBO journal [EMBO J] 2020 Apr 15; Vol. 39 (8), pp. e104120. Date of Electronic Publication: 2020 Mar 03.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
Język:
English
Imprint Name(s):
Publication: 2014- : London : Wiley Blackwell
Original Publication: Eynsham, Oxford, England : Published for the European Molecular Biology Organization by IRL Press, [c1982-
MeSH Terms:
Alkyl and Aryl Transferases/*metabolism
Dimethylallyltranstransferase/*metabolism
R-SNARE Proteins/*metabolism
SNARE Proteins/*metabolism
Alkyl and Aryl Transferases/chemistry ; Alkyl and Aryl Transferases/genetics ; Animals ; Dimethylallyltranstransferase/chemistry ; Dimethylallyltranstransferase/genetics ; Golgi Apparatus/metabolism ; Humans ; Male ; Membrane Fusion ; Protein Binding ; Protein Multimerization ; Protein Prenylation ; Protein Transport ; R-SNARE Proteins/genetics ; Rats ; Rats, Wistar
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Grant Information:
16K08574 International MEXT | Japan Society for the Promotion of Science (JSPS); 17K15072 International MEXT | Japan Society for the Promotion of Science (JSPS); 16H05148 International MEXT | Japan Society for the Promotion of Science (JSPS); International Takeda Science Foundation; JPMJCR12M5 International MEXT | JST | Core Research for Evolutional Science and Technology (CREST)
Contributed Indexing:
Keywords: SNARE; Golgi; PTAR1; Ykt6; protein prenylation
Molecular Sequence:
PDB 6J6X; 6J74; 6J7X; 6J7F
Substance Nomenclature:
0 (R-SNARE Proteins)
0 (SNARE Proteins)
0 (YKT6 protein, human)
EC 2.5.- (Alkyl and Aryl Transferases)
EC 2.5.- (RABGGTB protein, human)
EC 2.5.1.1 (Dimethylallyltranstransferase)
EC 2.5.1.1 (PTAR1 protein, human)
Entry Date(s):
Date Created: 20200305 Date Completed: 20201214 Latest Revision: 20210415
Update Code:
20240105
PubMed Central ID:
PMC7156963
DOI:
10.15252/embj.2019104120
PMID:
32128853
Czasopismo naukowe
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.
(© 2020 The Authors.)
Comment in: EMBO J. 2020 Apr 15;39(8):e104744. (PMID: 32202660)

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