PRMT5 regulates Golgi apparatus structure through methylation of the golgin GM130.
Maintenance of the Golgi apparatus (GA) structure and function depends on Golgi matrix proteins. The posttranslational modification of Golgi proteins such as phosphorylation of members of the golgin and GRASP families is important for determining Golgi architecture. Some Golgi proteins including golgin-84 are also known to be methylated, but the function of golgin methylation remains unclear. Here, we show that the protein arginine methyltransferase 5 (PRMT5) localizes to the GA and forms complexes with several components involved in GA ribbon formation and vesicle tethering. PRMT5 interacts with the golgin GM130, and depletion of PRMT5 causes defects in Golgi ribbon formation. Furthermore, PRMT5 methylates N-terminal arginines in GM130, and such arginine methylation appears critical for GA ribbon formation. Our findings reveal a molecular mechanism by which PRMT5-dependent arginine methylation of GM130 controls the maintenance of GA architecture.
Zhou
Zhongwei
Z
Key Laboratory of Molecular and Developmental Biology, Institute of Genetics and Developmental Biology (IGDB), Chinese Academy of Sciences, Beijing 100101, China.
Sun
Xiaotian
X
Zou
Zhenhua
Z
Sun
Litao
L
Zhang
Tao
T
Guo
Shaoshi
S
Wen
Ya
Y
Liu
Lin
L
Wang
Yi
Y
Qin
Jun
J
Li
Lei
L
Gong
Weimin
W
Bao
Shilai
S
D001120:Arginine / Q000378:metabolism; D001324:Autoantigens / Q000378:metabolism*; D045744:Cell Line, Tumor; D006056:Golgi Apparatus / Q000737:chemistry / Q000201:enzymology* / Q000648:ultrastructure; D006801:Humans; D008565:Membrane Proteins / Q000378:metabolism*; D008745:Methylation; D011496:Protein Methyltransferases / Q000032:analysis / Q000235:genetics / Q000378:metabolism*; D011484:Protein-Arginine N-Methyltransferases; D034622:RNA Interference
D001324:Autoantigens; C097741:Golgin subfamily A member 2; D008565:Membrane Proteins; D001120:Arginine; D011496:Protein Methyltransferases; C400529:PRMT5 protein, human; D011484:Protein-Arginine N-Methyltransferases