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Anfractuous assemblies of IMP dehydrogenase and CTP synthase: new twists on regulation?
Author(s) -
McCluskey Gregory D.,
Bearne Stephen L.
Publication year - 2018
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.14658
Subject(s) - atp synthase , chemistry , dehydrogenase , biochemistry , microbiology and biotechnology , enzyme , biology
CTP synthase (CTPS) and IMP dehydrogenase (IMPDH) catalyse the rate‐limiting steps of de novo CTP and guanosine nucleotide biosynthesis, respectively, and form filament assemblies in response to inhibitors. A recent study explores the morphology and dynamics of these assemblies using fluorescence and super‐resolution confocal microscopy with cell lines expressing CTPS1 and IMPDH2 fusion proteins. The formation and dismantling of mixed assemblies depends on nucleotide levels, suggesting a co‐regulation function.