Alt. symbols: EFTUD1 | FLJ13119 | FAM42A | HsT19294 | RIA1

Approved name: elongation factor like GTPase 1
Alt. names: elongation factor Tu GTP binding domain containing 1 | ribosome assembly 1 homolog (yeast)

Location: 15q25.2: 82130206 - 82262773 (-)
Gene type: protein_coding, 17 transcripts.

Scores: LoFtool: 0.756000 | pLI: 0.03365568 | LOEUF: 0.561

HGNC: 25789

NCBI: 79631, RefSeq: .0

Ensembl: ENSG00000140598.16

LRG_ | Status: none

OMIM: 617538

Expression | ProteinAtlas

The protein encoded by EFL1 is involved in the biogenesis of the 60S ribosomal subunit and translational activation of ribosomes. During ribosome biogenesis nascent 40S and 60S subunits are exported to the cell cytoplasm to face the last maturation steps. To prevent premature association of these ribosomal subunits, eukaryotic initiation factor 6 (eIF6) binds the 60S subunit within the nucleus. Once in the cytoplasm, eiF6 is released from the 60S subunit by the interaction of EFL1 and SDBS proteins. This release activates ribosomes for translation competence by allowing 80S ribosome assembly and facilitating EIF6 recycling to the nucleus, where it is required for 60S rRNA processing and nuclear export. Studies with the yeast orthologue efl1 suggest that SBDS protein may act as a guanine nucleotide exchange factor (GEF) for EFL1 favouring a conformation of low affinity for guanosine diphosphate (GDP). EFL1 has low intrinsic GTPase activity, which is increased by contact with 60S ribosome subunits.

To date at least 9 individuals from 5 unrelated families have been reported in the literature with Shwachman-Diamond or Shwachman-Diamond like syndrome and biallelic mutations in EFL1 (Stepensky P et al. 2017; Tan S et al. 2019). The mutations identified in these patients are p.M882K, p.R1095Q, p.F505S, p.C883G, p.R970H, and the nonsense mutation p.R754*. Stepensky and colleagues (2017) showed that mutant EFL1 proteins do not promote the release of cytoplasmic Tif6 (eIF6 orthologue) from the 60S subunit in yeast cells, likely preventing the formation of mature ribosomes. Tif6-GFP was re-localised to the cytoplasm in mutant yeast cells, instead of remaining in the nucleus. Tan S and colleagues (2019) also proved impaired ribosomal subunit joining and attenuated global protein translation as a consequence of defective eIF6 eviction. [Load More]