EEF1G — Eukaryotic Translation Elongation Factor 1 Gamma

EEF1G — Eukaryotic Translation Elongation Factor 1 Gamma

Introduction

EEF1G (Eukaryotic Translation Elongation Factor 1 Gamma) is a critical subunit of the eukaryotic translation elongation factor 1 (EF-1) complex, which is essential for protein synthesis in all eukaryotic cells. The EF-1 complex mediates the delivery of aminoacyl-tRNAs to the ribosome during the elongation phase of translation, making it fundamental for cellular protein homeostasis.

Gene Information

<div class="infobox infobox-gene">
<table>
<tr><th>Symbol</th><td>EEF1G</td></tr>
<tr><th>Full Name</th><td>Eukaryotic Translation Elongation Factor 1 Gamma</td></tr>
<tr><th>Aliases</th><td>EF-1γ, EF1G</td></tr>
<tr><th>Chromosomal Location</th><td>Chr11q12.3</td></tr>
<tr><th>NCBI Gene ID</th><td>1939</td></tr>
<tr><th>Ensembl ID</th><td>ENSG00000185208</td></tr>
<tr><th>UniProt ID</th><td>P26641</td></tr>
<tr><th>Associated Diseases</th><td>ALS, Alzheimer's Disease, Parkinson's Disease, Neurodegeneration, Cancer</td></tr>
</table>
</div>

Function

EF-1 Complex Structure

The EF-1 complex consists of five subunits[@andersen2003]:

• EEF1A (α): The GTP-binding protein that delivers aminoacyl-tRNAs
• EEF1B (β): Guanine nucleotide exchange factor
• EEF1D (δ): Another exchange factor subunit
• EEF1G (γ): Structural and regulatory subunit
• EEF1E1 (ε): Associated factor

Translation Elongation

EEF1G plays several essential roles in translation[@negrutskii1998]:

EEF1G — Eukaryotic Translation Elongation Factor 1 Gamma

Introduction

EEF1G (Eukaryotic Translation Elongation Factor 1 Gamma) is a critical subunit of the eukaryotic translation elongation factor 1 (EF-1) complex, which is essential for protein synthesis in all eukaryotic cells. The EF-1 complex mediates the delivery of aminoacyl-tRNAs to the ribosome during the elongation phase of translation, making it fundamental for cellular protein homeostasis.

Gene Information

<div class="infobox infobox-gene">
<table>
<tr><th>Symbol</th><td>EEF1G</td></tr>
<tr><th>Full Name</th><td>Eukaryotic Translation Elongation Factor 1 Gamma</td></tr>
<tr><th>Aliases</th><td>EF-1γ, EF1G</td></tr>
<tr><th>Chromosomal Location</th><td>Chr11q12.3</td></tr>
<tr><th>NCBI Gene ID</th><td>1939</td></tr>
<tr><th>Ensembl ID</th><td>ENSG00000185208</td></tr>
<tr><th>UniProt ID</th><td>P26641</td></tr>
<tr><th>Associated Diseases</th><td>ALS, Alzheimer's Disease, Parkinson's Disease, Neurodegeneration, Cancer</td></tr>
</table>
</div>

Function

EF-1 Complex Structure

The EF-1 complex consists of five subunits[@andersen2003]:

• EEF1A (α): The GTP-binding protein that delivers aminoacyl-tRNAs
• EEF1B (β): Guanine nucleotide exchange factor
• EEF1D (δ): Another exchange factor subunit
• EEF1G (γ): Structural and regulatory subunit
• EEF1E1 (ε): Associated factor

Translation Elongation

EEF1G plays several essential roles in translation[@negrutskii1998]:

Cellular Functions Beyond Translation

Emerging research indicates EEF1G has additional cellular functions[@ejiri2002]:

• Cytoskeletal interactions: Associates with microtubules and actin filaments
• Signal transduction: Involved in cellular signaling pathways
• [Apoptosis](/entities/apoptosis) regulation: Modulates programmed cell death pathways

Role in Neurodegenerative Diseases

Amyotrophic Lateral Sclerosis (ALS)

EEF1G has been strongly implicated in ALS pathogenesis[@chen2004][@dropiewska2015]:

• Dysregulated expression: Altered EEF1G levels in motor [neurons](/entities/neurons) of ALS patients
• Stress granule formation: Participates in stress granule dynamics, which are disrupted in ALS
• Protein homeostasis: Essential for maintaining proper translation under cellular stress
• TDP-43 pathology: Interaction with [TDP-43 protein](/mechanisms/tdp-43-proteinopathy) aggregates

Alzheimer's Disease

In [Alzheimer's disease](/diseases/alzheimers-disease), EEF1G dysfunction contributes to[@ma2012]:

• Translation impairment: Global translation deficits in AD brains
• Synaptic protein synthesis: Disrupted local translation at synapses
• Memory consolidation: Impaired protein synthesis required for memory formation
• ER stress: Contributes to endoplasmic reticulum stress response

Parkinson's Disease

EEF1G alterations in PD include[@liu2020]:

• Mitochondrial protein synthesis: Impaired translation of mitochondrial proteins
• [Alpha-synuclein](/proteins/alpha-synuclein) toxicity: May influence alpha-synuclein aggregation pathways
• Neuroprotection loss: Reduced ability to respond to cellular stress

Other Neurodegenerative Conditions

• Huntington's disease: Translation dysregulation affecting mutant [huntingtin](/proteins/huntingtin) clearance
• Frontotemporal dementia: Stress granule abnormalities
• Spinocerebellar ataxias: Translation factor mutations

Structure

EEF1G (P26641) is a 437 amino acid protein with:

• N-terminal domain: Interaction with other EF-1 subunits
• C-terminal domain: GTPase-activating protein (GAP) homology region
• Multiple phosphorylation sites: Regulatory control points

Clinical Significance

ALS Associations

EEF1G is considered a potential therapeutic target in ALS[@kim2020]:

• Gene expression modifiers
• Biomarker potential for disease progression
• Modulation of stress response pathways

Cancer

Paradoxically, EEF1G is overexpressed in various cancers, highlighting its importance in cell proliferation and survival[@edmunds2002].

Therapeutic Implications

Understanding EEF1G function provides opportunities for therapeutic intervention:

• Translation modulators: Small molecules targeting EF-1 complex function
• Stress granule inhibitors: Addressing abnormal granule dynamics
• Gene therapy approaches: Restoring proper translation homeostasis

See Also

• [EF1A1](/genes/ef1a1)
• [EIF2AK2](/genes/eif2ak2)
• [Translation Elongation](/mechanisms/translation-elongation)
• [Protein Synthesis](/mechanisms/protein-synthesis)
• [Stress Granules](/mechanisms/stress-granules)

External Links

• [NCBI Gene: EEF1G](https://www.ncbi.nlm.nih.gov/gene/1939)
• [UniProt: EEF1G](https://www.uniprot.org/uniprot/P26641)

References