ReviewRNA (New York, N.Y.)2022
A working model for condensate RNA-binding proteins as matchmakers for protein complex assembly.
Review in RNA (New York, N.Y.), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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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
20 citing papers in PubMed, 31 citations in OpenAlex.
- Integrative profiling of condensation-prone RNAs during early development.Cell genomics · 2026Article
- The RNA-binding protein RNP1A is essential and interacts with contractility kit proteins to facilitate cell mechanics.Journal of cell science · 2026Article
- Synthetic biomolecular condensates enhance translation from a target mRNA in living cells.Nature chemistry · 2025Article
- Article
- Multi-protein assemblies orchestrate co-translational enzymatic processing on the human ribosome.Nature communications · 2024Article
- Mapping RNA-protein interactions with subcellular resolution using colocalization CLIP.RNA (New York, N.Y.) · 2024Article
- The FXR1 network acts as signaling scaffold for actomyosin remodeling.bioRxiv : the preprint server for biology · 2024Article
- FMRP-mediated spatial regulation of physiologic NMD targets in neuronal cells.Genome biology · 2024Review
- Buffering of genetic dominance by allele-specific protein complex assembly.Science advances · 2023Article
- RNA granules: functional compartments or incidental condensates?Genes & development · 2023Review
- A cell-type-specific alternative splicing regulator shapes synapse properties in a trans-synaptic manner.Cell reports · 2023Article
- mRNA interactions with disordered regions control protein activity.bioRxiv : the preprint server for biology · 2023Article
- Context-specific regulation and function of mRNA alternative polyadenylation.Nature reviews. Molecular cell biology · 2022Review
- Cotranslational Mechanisms of Protein Biogenesis and Complex Assembly in Eukaryotes.Annual review of biomedical data science · 2022Review
- Article
- Stress-induced perturbations in intracellular amino acids reprogram mRNA translation in osmoadaptation independently of the ISR.Cell reports · 2022Article
- Extended disordered regions of ribosome-associated NAC proteins paralogs belong only to the germline in Drosophila melanogaster.Scientific reports · 2022Article
- The dual nature of the nucleolus.Genes & development · 2022Review
- Keeping up with the condensates: The retention, gain, and loss of nuclear membrane-less organelles.Frontiers in molecular biosciences · 2022Review
- The DNA binding high mobility group box protein family functionally binds RNA.Wiley interdisciplinary reviews. RNAReview
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Most cellular processes are carried out by protein complexes, but it is still largely unknown how the subunits of lowly expressed complexes find each other in the crowded cellular environment. Here, we will describe a working model where RNA-binding proteins in cytoplasmic condensates act as matchmakers between their bound proteins (called protein targets) and newly translated proteins of their RNA targets to promote their assembly into complexes. Different RNA-binding proteins act as scaffolds for various cytoplasmic condensates with several of them supporting translation. mRNAs and proteins are recruited into the cytoplasmic condensates through binding to specific domains in the RNA-binding proteins. Scaffold RNA-binding proteins have a high valency. In our model, they use homotypic interactions to assemble condensates and they use heterotypic interactions to recruit protein targets into the condensates. We propose that unoccupied binding sites in the scaffold RNA-binding proteins transiently retain recruited and newly translated proteins in the condensates, thus promoting their assembly into complexes. Taken together, we propose that lowly expressed subunits of protein complexes combine information in their mRNAs and proteins to colocalize in the cytoplasm. The efficiency of protein complex assembly is increased by transient entrapment accomplished by multivalent RNA-binding proteins within cytoplasmic condensates.
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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.