ArticleThe Journal of cell biology2024
hGRAD: A versatile "one-fits-all" system to acutely deplete RNA binding proteins from condensates.
Article in The Journal of cell biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 8 citations in OpenAlex.
- A new rapid-degradation system combined with super-resolution microscopy.Nature reviews. Molecular cell biology · 2025Article
- Rapid depletion and super-resolution microscopy reveal dual roles of SRSF5 in coordinating nuclear speckle-paraspeckle crosstalk during cellular stress.Nucleic acids research · 2025Article
- Genetically encoded affinity reagents are a toolkit for visualizing and manipulating endogenous protein function in vivo.Nature communications · 2025Article
- Arid5a uses disordered extensions of its core ARID domain for distinct DNA- and RNA-recognition and gene regulation.The Journal of biological chemistry · 2024Article
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
Nuclear RNA binding proteins (RBPs) are difficult to study because they often belong to large protein families and form extensive networks of auto- and crossregulation. They are highly abundant and many localize to condensates with a slow turnover, requiring long depletion times or knockouts that cannot distinguish between direct and indirect or compensatory effects. Here, we developed a system that is optimized for the rapid degradation of nuclear RBPs, called hGRAD. It comes as a "one-fits-all" plasmid, and integration into any cell line with endogenously GFP-tagged proteins allows for an inducible, rapid, and complete knockdown. We show that the nuclear RBPs SRSF3, SRSF5, SRRM2, and NONO are completely cleared from nuclear speckles and paraspeckles within 2 h. hGRAD works in various cell types, is more efficient than previous methods, and does not require the expression of exogenous ubiquitin ligases. Combining SRSF5 hGRAD degradation with Nascent-seq uncovered transient transcript changes, compensatory mechanisms, and an effect of SRSF5 on transcript stability.
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Registered trials
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