Phosphorylation of Serine 51 in Initiation Factor 2α (eIF2α) Promotes Complex Formation between eIF2α(P) and eIF2B and Causes Inhibition in the Guanine Nucleotide Exchange Activity of eIF2B

Sudhakar, Akulapalli; Ramachandran, Aruna; Ghosh, Sudip; E. Hasnain, Seyed; J. Kaufman, Randal; V.A. Ramaiah, Kolluru

doi:10.1021/bi0008682

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Phosphorylation of Serine 51 in Initiation Factor 2α (eIF2α) Promotes Complex Formation between eIF2α(P) and eIF2B and Causes Inhibition in the Guanine Nucleotide Exchange Activity of eIF2B

Published in Biochemistry • Sep 27, 2000

Authors:

Akulapalli Sudhakar

Aruna Ramachandran

Sudip Ghosh

Abstract

Phosphorylation of serine 51 residue on the alpha-subunit of eukaryotic initiation factor 2 (eIF2alpha) inhibits the guanine nucleotide exchange (GNE) activity of eIF2B, presumably, by forming a tight complex with eIF2B. Inhibition of the GNE activity of eIF2B leads to impairment in eIF2 recycling a...

Subject

eIF2

EIF-2 kinase

Eukaryotic initiation factor

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