Ubiquitination and filamentous structure of cytidine triphosphate synthase

Li Mei Pai, Pei Yu Wang, Wei Cheng Lin, Archan Chakraborty, Chau Ting Yeh, Yu Hung Lin

Research output: Contribution to journalComment/debate

7 Citations (Scopus)


Living organisms respond to nutrient availability by regulating the activity of metabolic enzymes. Therefore, the reversible post-translational modification of an enzyme is a common regulatory mechanism for energy conservation. Recently, cytidine-5′-triphosphate (CTP) synthase was discovered to form a filamentous structure that is evolutionarily conserved from flies to humans. Interestingly, induction of the formation of CTP synthase filament is responsive to starvation or glutamine depletion. However, the biological roles of this structure remain elusive. We have recently shown that ubiquitination regulates CTP synthase activity by promoting filament formation in Drosophila ovaries during endocycles. Intriguingly, although the ubiquitination process was required for filament formation induced by glutamine depletion, CTP synthase ubiquitination was found to be inversely correlated with filament formation in Drosophila and human cell lines. In this article, we discuss the putative dual roles of ubiquitination, as well as its physiological implications, in the regulation of CTP synthase structure.

Original languageEnglish
Pages (from-to)108-114
Number of pages7
Issue number3
Publication statusPublished - 2016 Jul 2

All Science Journal Classification (ASJC) codes

  • Insect Science

Fingerprint Dive into the research topics of 'Ubiquitination and filamentous structure of cytidine triphosphate synthase'. Together they form a unique fingerprint.

Cite this