Arabidopsis lysin motif/F‐box‐containing protein InLYP1 fine‐tunes glycine metabolism by degrading glycine decarboxylase GLDP2

2021 ◽  
Author(s):  
Jianhang Guo ◽  
Ben‐Qiang Gong ◽  
Jian‐Feng Li
2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Rui Liu ◽  
Lin-Wen Zeng ◽  
Rong Gong ◽  
Fanen Yuan ◽  
Hong-Bing Shu ◽  
...  

AbstractGlycine decarboxylase (GLDC) is a key enzyme of glycine cleavage system that converts glycine into one-carbon units. GLDC is commonly up-regulated and plays important roles in many human cancers. Whether and how GLDC is regulated by post-translational modifications is unknown. Here we report that mechanistic target of rapamycin complex 1 (mTORC1) signal inhibits GLDC acetylation at lysine (K) 514 by inducing transcription of the deacetylase sirtuin 3 (SIRT3). Upon inhibition of mTORC1, the acetyltransferase acetyl-CoA acetyltransferase 1 (ACAT1) catalyzes GLDC K514 acetylation. This acetylation of GLDC impairs its enzymatic activity. In addition, this acetylation of GLDC primes for its K33-linked polyubiquitination at K544 by the ubiquitin ligase NF-X1, leading to its degradation by the proteasomal pathway. Finally, we find that GLDC K514 acetylation inhibits glycine catabolism, pyrimidines synthesis and glioma tumorigenesis. Our finding reveals critical roles of post-translational modifications of GLDC in regulation of its enzymatic activity, glycine metabolism and tumorigenesis, and provides potential targets for therapeutics of cancers such as glioma.


1990 ◽  
Vol 80 (3) ◽  
pp. 487-491 ◽  
Author(s):  
David J. Oliver ◽  
Michel Neuburger ◽  
Jacques Bourguignon ◽  
Roland Douce

1967 ◽  
Vol 242 (2) ◽  
pp. 301-305 ◽  
Author(s):  
Sigrid M. Klein ◽  
Richard D. Sagers
Keyword(s):  

1966 ◽  
Vol 241 (1) ◽  
pp. 206-209
Author(s):  
Sigrid M. Klein ◽  
Richard D. Sagers
Keyword(s):  

1994 ◽  
Vol 104 (3) ◽  
pp. 1077-1078 ◽  
Author(s):  
S. Kopriva ◽  
H. Bauwe

1977 ◽  
Vol 78 (2) ◽  
pp. 483-491 ◽  
Author(s):  
A.L. Moore ◽  
C. Jackson ◽  
B. Halliwell ◽  
J.E. Dench ◽  
D.O. Hall

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