Ferriheme dissociates from p-T-EIF2AK1:2xferriheme dimer

Stable Identifier
R-OCU-9655573
Type
Reaction [dissociation]
Species
Oryctolagus cuniculus
Compartment
ReviewStatus
5/5
General
SVG |   | PPTX  | SBGN
Ferriheme dissociates from p-T-EIF2AK1:2xferriheme dimer
One molecule of hemin (ferriheme b chloride) tightly binds the N-terminal domain of EIF2AK1 (HRI) and one molecule of hemin loosely binds the kinase insert (KI) domain of EIF2AK1 (Chefalo et al. 1998, Rafie-Kolpin et al. 2000). When cytosolic heme concentrations are low, heme dissociates from the KI domain, resulting in activation of the kinase activity of EIF2AK1 (Rafie-Kolpin et al. 2000).
Literature References
PubMed ID Title Journal Year
9874252 Heme-regulated eIF-2alpha kinase purifies as a hemoprotein

Rafie-Kolpin, M, Chen, JJ, Oh, J, Kan, B, Chefalo, PJ

Eur. J. Biochem. 1998
10671563 Two heme-binding domains of heme-regulated eukaryotic initiation factor-2alpha kinase. N terminus and kinase insertion

Uma, S, Rafie-Kolpin, M, Hahn, J, Chen, JJ, Hussain, Z, Chefalo, PJ, Matts, RL

J. Biol. Chem. 2000
Participants
Orthologous Events
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