7T0Y

The Ribosomal RNA Processing 1B Protein Phosphatase-1 Holoenzyme

7T0Y の概要

• エントリーDOI: 10.2210/pdb7t0y/pdb
• 分子名称: Serine/threonine-protein phosphatase PP1-alpha catalytic subunit, Ribosomal RNA processing protein 1 homolog B, 1,2-ETHANEDIOL, ... (7 entities in total)
• 機能のキーワード: protein binding, hydrolase
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 79901.73

構造登録者

Srivastava, G.,Page, R.,Peti, W. (登録日: 2021-11-30, 公開日: 2022-12-07, 最終更新日: 2023-10-25)

主引用文献

Srivastava, G.,Bajaj, R.,Kumar, G.S.,Gaudreau-Lapierre, A.,Nicolas, H.,Chamousset, D.,Kreitler, D.,Peti, W.,Trinkle-Mulcahy, L.,Page, R.
The ribosomal RNA processing 1B:protein phosphatase 1 holoenzyme reveals non-canonical PP1 interaction motifs.
Cell Rep, 41:111726-111726, 2022

PubMed Abstract: The serine/threonine protein phosphatase 1 (PP1) dephosphorylates hundreds of substrates by associating with >200 regulatory proteins to form specific holoenzymes. The major PP1 targeting protein in the nucleolus is RRP1B (ribosomal RNA processing 1B). In addition to selectively recruiting PP1β/PP1γ to the nucleolus, RRP1B also has a key role in ribosome biogenesis, among other functions. How RRP1B binds PP1 and regulates nucleolar phosphorylation signaling is not yet known. Here, we show that RRP1B recruits PP1 via established (RVxF/SILK/ΦΦ) and non-canonical motifs. These atypical interaction sites, the PP1β/γ specificity, and N-terminal AF-binding pockets rely on hydrophobic interactions that contribute to binding and, via phosphorylation, regulate complex formation. This work advances our understanding of PP1 isoform selectivity, reveals key roles of N-terminal PP1 residues in regulator binding, and suggests that additional PP1 interaction sites have yet to be identified, all of which are necessary for a systems biology understanding of PP1 function.

PubMed: 36450254
DOI: 10.1016/j.celrep.2022.111726

実験手法

X-RAY DIFFRACTION (1.8 Å)