ArticleGenes & development2010
ZBP1 recognition of beta-actin zipcode induces RNA looping.
Article in Genes & development, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 122 papers.
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Who cites it
122 citing papers in PubMed, 206 citations in OpenAlex.
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- Novel insights into the interaction between IGF2BPs and ncRNAs in cancers.Cancer cell international · 2024Review
- An image-based RNAi screen identifies the EGFR signaling pathway as a regulator of Imp RNP granules.Journal of cell science · 2024Article
- IGF2BP1 phosphorylation in the disordered linkers regulates ribonucleoprotein condensate formation and RNA metabolism.Nature communications · 2024Article
- Interactive Structural Analysis of KH3-4 Didomains of IGF2BPs with Preferred RNA Motif Having mInternational journal of molecular sciences · 2024Article
- Identification of RNA structures and their roles in RNA functions.Nature reviews. Molecular cell biology · 2024Review
- RNA NNature reviews. Urology · 2024Review
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- GCLiPP: global crosslinking and protein purification method for constructing high-resolution occupancy maps for RNA binding proteins.Genome biology · 2023Article
- Direct m6A recognition by IMP1 underlays an alternative model of target selection for non-canonical methyl-readers.Nucleic acids research · 2023Article
- Bioinformatics analysis and verification of m6A related genes based on the construction of keloid diagnostic model.International wound journal · 2023Article
62 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
ZBP1 (zipcode-binding protein 1) was originally discovered as a trans-acting factor for the "zipcode" in the 3' untranslated region (UTR) of the beta-actin mRNA that is important for its localization and translational regulation. Subsequently, ZBP1 has been found to be a multifunctional regulator of RNA metabolism that controls aspects of localization, stability, and translation for many mRNAs. To reveal how ZBP1 recognizes its RNA targets, we biochemically characterized the interaction between ZBP1 and the beta-actin zipcode. The third and fourth KH (hnRNP K homology) domains of ZBP1 specifically recognize a bipartite RNA element located within the first 28 nucleotides of the zipcode. The spacing between the RNA sequences is consistent with the structure of IMP1 KH34, the human ortholog of ZBP1, that we solved by X-ray crystallography. The tandem KH domains are arranged in an intramolecular anti-parallel pseudodimer conformation with the canonical RNA-binding surfaces at opposite ends of the molecule. This orientation of the KH domains requires that the RNA backbone must undergo an approximately 180 degrees change in direction in order for both KH domains to contact the RNA simultaneously. The RNA looping induced by ZBP1 binding provides a mechanism for specific recognition and may facilitate the assembly of post-transcriptional regulatory complexes by remodeling the bound transcript.
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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.