ArticleProceedings of the National Academy of Sciences of the United States of America2022
Cotranslational interaction of human EBP50 and ezrin overcomes masked binding site during complex assembly.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
5 citing papers in PubMed, 8 citations in OpenAlex.
- Cotranslational assembly directs the biogenesis of the mProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Evaluation of nanoparticle albumin-bound paclitaxel loaded macrophages for glioblastoma treatment based on a microfluidic chip.Frontiers in bioengineering and biotechnology · 2024Article
- Benefits of co-translational complex assembly for cellular fitness.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023Article
- Ezrin expression in female reproductive tissues: A review of regulation and pathophysiological implications.Frontiers in cell and developmental biology · 2023Review
- Multimodal cotranslational interactions direct assembly of the human multi-tRNA synthetase complex.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Multiprotein assemblages are the intracellular workhorses of many physiological processes. Assembly of constituents into complexes can be driven by stochastic, domain-dependent, posttranslational events in which mature, folded proteins specifically interact. However, inaccessibility of interacting surfaces in mature proteins (e.g., due to "buried" domains) can obstruct complex formation. Mechanisms by which multiprotein complex constituents overcome topological impediments remain enigmatic. For example, the heterodimeric complex formed by EBP50 and ezrin must address this issue as the EBP50-interacting domain in ezrin is obstructed by a self-interaction that occupies the EBP50 binding site. Here, we show that the EBP50-ezrin complex is formed by a cotranslational mechanism in which the C terminus of mature, fully formed EBP50 binds the emerging, ribosome-bound N-terminal FERM domain of ezrin during
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.