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

Stable Identifier
R-HSA-9648880
Type
Reaction [dissociation]
Species
Homo sapiens
Compartment
Locations in the PathwayBrowser
General
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

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 (Bhavnani et al. 2018, and inferred from rabbit and mouse homologs). When cytosolic heme concentrations are low, heme dissociates from the KI domain, resulting in activation of the kinase activity of EIF2AK1 (inferred from rabbit and mouse homologs).

Literature References
PubMed ID Title Journal Year
28814160 Elucidation of molecular mechanism of stability of the heme-regulated eIF2α kinase upon binding of its ligand, hemin in its catalytic kinase domain

Bhavnani, V, Kaviraj, S, Panigrahi, P, Suresh, CG, Yapara, S, Pal, J

J. Biomol. Struct. Dyn. 2018
Participants
Participant Of
Inferred From
Authored
Reviewed
Created
Cite Us!