Ontology highlight
ABSTRACT:
SUBMITTER: Walden M
PROVIDER: S-EPMC6914362 | biostudies-literature | 2019 Jun
REPOSITORIES: biostudies-literature
Walden Miriam M Tian Lei L Ross Rebecca L RL Sykora Upasana M UM Byrne Dominic P DP Hesketh Emma L EL Masandi Safi K SK Cassel Joel J George Rachel R Ault James R JR El Oualid Farid F Pawłowski Krzysztof K Salvino Joseph M JM Eyers Patrick A PA Ranson Neil A NA Del Galdo Francesco F Greenberg Roger A RA Zeqiraj Elton E
Nature 20190529 7760
Serine hydroxymethyltransferase 2 (SHMT2) regulates one-carbon transfer reactions that are essential for amino acid and nucleotide metabolism, and uses pyridoxal-5'-phosphate (PLP) as a cofactor. Apo SHMT2 exists as a dimer with unknown functions, whereas PLP binding stabilizes the active tetrameric state. SHMT2 also promotes inflammatory cytokine signalling by interacting with the deubiquitylating BRCC36 isopeptidase complex (BRISC), although it is unclear whether this function relates to metab ...[more]