EIF4G1

The protein encoded by this gene is a component of the multi-subunit protein complex EIF4F. This complex facilitates the recruitment of mRNA to the ribosome, which is a rate-limiting step during the initiation phase of protein synthesis. The recognition of the mRNA cap and the ATP-dependent unwinding of 5'-terminal secondary structure is catalyzed by factors in this complex. The subunit encoded by this gene is a large scaffolding protein that contains binding sites for other members of the EIF4F complex. A domain at its N-terminus can also interact with the poly(A)-binding protein, which may mediate the circularization of mRNA during translation. Alternative splicing results in multiple transcript variants, some of which are derived from alternative promoter usage. [provided by RefSeq, Aug 2010]

Full Name

Eukaryotic Translation Initiation Factor 4 Gamma 1

Research Area

Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome. As a member of the eIF4F complex, required for endoplasmic reticulum stress-induced ATF4 mRNA translation (PubMed:29062139).

Biological Process

Behavioral fear response Source: Ensembl
Cap-dependent translational initiation Source: ParkinsonsUK-UCL
Cellular macromolecule biosynthetic process Source: ParkinsonsUK-UCL
Cellular response to nutrient levels Source: ParkinsonsUK-UCL
Developmental process Source: ParkinsonsUK-UCL
Energy homeostasis Source: ParkinsonsUK-UCL
Negative regulation of autophagy Source: ParkinsonsUK-UCL
Negative regulation of neuron death Source: ParkinsonsUK-UCL
Negative regulation of peptidyl-threonine phosphorylation Source: ParkinsonsUK-UCL
Positive regulation of cell death Source: ParkinsonsUK-UCL
Positive regulation of cell growth Source: ParkinsonsUK-UCL
Positive regulation of cellular protein metabolic process Source: ParkinsonsUK-UCL
Positive regulation of eukaryotic translation initiation factor 4F complex assembly Source: ParkinsonsUK-UCL
Positive regulation of G1/S transition of mitotic cell cycle Source: ParkinsonsUK-UCL
Positive regulation of miRNA mediated inhibition of translation Source: ParkinsonsUK-UCL
Positive regulation of mRNA cap binding Source: ParkinsonsUK-UCL
Positive regulation of neuron differentiation Source: Ensembl
Positive regulation of peptidyl-serine phosphorylation Source: ParkinsonsUK-UCL
Positive regulation of translation in response to endoplasmic reticulum stress Source: UniProtKB
Regulation of cellular response to stress Source: ParkinsonsUK-UCL
Regulation of gene silencing by miRNA Source: ParkinsonsUK-UCL
Regulation of polysome binding Source: ParkinsonsUK-UCL
Regulation of presynapse assembly Source: ParkinsonsUK-UCL
Regulation of translational initiation Source: UniProtKB
Translation Source: ParkinsonsUK-UCL
Translational initiation Source: ParkinsonsUK-UCL

Cellular Location

Stress granule

Involvement in disease

Parkinson disease 18 (PARK18):
An autosomal dominant, late-onset form of Parkinson disease. Parkinson disease is a complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity and postural instability, as well as by a clinically significant response to treatment with levodopa. The pathology involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain.

PTM

Phosphorylated at multiple sites in vivo. Phosphorylation at Ser-1185 by PRKCA induces binding to MKNK1.
Following infection by certain enteroviruses, rhinoviruses and aphthoviruses, EIF4G1 is cleaved by the viral protease 2A, or the leader protease in the case of aphthoviruses. This shuts down the capped cellular mRNA transcription.