ArticleActa crystallographica. Section F, Structural biology communications2018
The structure of SDS22 provides insights into the mechanism of heterodimer formation with PP1.
Article in Acta crystallographica. Section F, Structural biology communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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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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Who cites it
3 citing papers in PubMed, 5 citations in OpenAlex.
- The protein phosphatase OsPP1a dephosphorylates and stabilizes CatC to scavenge excess HPlant communications · 2026Article
- Role of Protein Phosphatase1 Regulatory Subunit3 in Mediating the Abscisic Acid Response.Plant physiology · 2020Article
- SDS22 selectively recognizes and traps metal-deficient inactive PP1.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
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Authors and funding
5 authors at 1 institution in 1 country.
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Abstract
Protein phosphatase 1 (PP1) dephosphorylates hundreds of key biological targets by associating with nearly 200 regulatory proteins to form highly specific holoenzymes. The vast majority of regulators are intrinsically disordered proteins (IDPs) and bind PP1 via short linear motifs within their intrinsically disordered regions. One of the most ancient PP1 regulators is SDS22, a protein that is conserved from yeast to mammals. Sequence analysis of SDS22 revealed that it is a leucine-rich repeat (LRR) protein, suggesting that SDS22, unlike nearly every other known PP1 regulator, is not an IDP but instead is fully structured. Here, the 2.9 Å resolution crystal structure of human SDS22 in space group P2
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