Evidence for interaction of 5,10-methylenetetrahydrofolate reductase (MTHFR) with methylenetetrahydrofolate dehydrogenase (MTHFD1) and general control nonderepressible 1 (GCN1)

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replicated interaction with both proteins. An AlphaFold 3 generated model of the MTHFR-MTHFD1 interaction places the MTHFD1 dehydrogenase/cyclohydrolase domain in direct contact with the MTHFR catalytic domain, suggesting their interaction may facilitate direct delivery of methylenetetrahydrofolate. Overall, we confirm methionine availability increases MTHFR phosphorylation, and identified potential interaction of MTHFR with MTHFD1 and GCN1.