ArticleNucleic acids research2013
Crystal structure of Cex1p reveals the mechanism of tRNA trafficking between nucleus and cytoplasm.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 14 citations in OpenAlex.
- Antibiotic target discovery by integrated phenotypic and activity-based profiling of electrophilic fragments.Cell chemical biology · 2025Article
- Functional annotation of proteins for signaling network inference in non-model species.Nature communications · 2023Article
- Evolution, structure and emerging roles of C1ORF112 in DNA replication, DNA damage responses, and cancer.Cellular and molecular life sciences : CMLS · 2021Review
- Cex1 is a component of the COPI intracellular trafficking machinery.Biology open · 2021Article
- MRB10130 is a RESC assembly factor that promotes kinetoplastid RNA editing initiation and progression.RNA (New York, N.Y.) · 2019Article
- Foreword to 'Multiscale structural biology: biophysical principles and mechanisms underlying the action of bio-nanomachines', a special issue in Honour of Fumio Arisaka's 70th birthday.Biophysical reviews · 2018Article
- Insights into the Structural Dynamics of Nucleocytoplasmic Transport of tRNA by Exportin-t.Biophysical journal · 2016Article
- Cytosolic Hsp70 and co-chaperones constitute a novel system for tRNA import into the nucleus.eLife · 2015Article
- A highly conserved region essential for NMD in the Upf2 N-terminal domain.Journal of molecular biology · 2014Article
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In all eukaryotes, transcribed precursor tRNAs are maturated by processing and modification processes in nucleus and are transported to the cytoplasm. The cytoplasmic export protein (Cex1p) captures mature tRNAs from the nuclear export receptor (Los1p) on the cytoplasmic side of the nuclear pore complex, and it delivers them to eukaryotic elongation factor 1α. This conserved Cex1p function is essential for the quality control of mature tRNAs to ensure accurate translation. However, the structural basis of how Cex1p recognizes tRNAs and shuttles them to the translational apparatus remains unclear. Here, we solved the 2.2 Å resolution crystal structure of Saccharomyces cerevisiae Cex1p with C-terminal 197 disordered residues truncated. Cex1p adopts an elongated architecture, consisting of N-terminal kinase-like and a C-terminal α-helical HEAT repeat domains. Structure-based biochemical analyses suggested that Cex1p binds tRNAs on its inner side, using the positively charged HEAT repeat surface and the C-terminal disordered region. The N-terminal kinase-like domain acts as a scaffold to interact with the Ran-exportin (Los1p·Gsp1p) machinery. These results provide the structural basis of Los1p·Gsp1p·Cex1p·tRNA complex formation, thus clarifying the dynamic mechanism of tRNA shuttling from exportin to the translational apparatus.
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