FDX1 regulates cellular protein lipoylation through direct binding to LIAS

Ferredoxins are a family of iron-sulfur (Fe-S) cluster proteins that serve as essential electron donors in numerous cellular processes that are conserved through evolution. The promiscuous nature of ferredoxins as electron donors enables them to participate in many metabolic processes including steroid, heme, vitamin D, and Fe-S cluster biosynthesis in different organisms. However, the unique natural function(s) of each of the two human ferredoxins (FDX1 and FDX2) are still poorly characterized. We recently reported that FDX1 is both a crucial regulator of copper ionophore-induced cell death and serves as an upstream regulator of cellular protein lipoylation, a mitochondrial lipid-based post-translational…

• NS
  National Science Foundation

  Awards: MCB-1716686, 1716686
• HH
  Howard Hughes Medical Institute
• BC
  Boston Children's Hospital
• NI
  National Institutes of Health

  Award: GM-122595
• NC
  National Cancer Institute

  Awards: R01CA279550, CA242457, 1 R35 CA242457-01