6EIH

The crystal structure of 14-3-3 epsilon in complex with the phosphorylated NELFE peptide

6EIH の概要

• エントリーDOI: 10.2210/pdb6eih/pdb
• 分子名称: 14-3-3 protein epsilon, SER-ILE-SEP-ARG (3 entities in total)
• 機能のキーワード: 14-3-3, nelf, protein binding
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 26913.56

構造登録者

Akutsu, M.,Wagner, S.A.,Beli, P. (登録日: 2017-09-19, 公開日: 2018-02-14, 最終更新日: 2024-11-20)

主引用文献

Borisova, M.E.,Voigt, A.,Tollenaere, M.A.X.,Sahu, S.K.,Juretschke, T.,Kreim, N.,Mailand, N.,Choudhary, C.,Bekker-Jensen, S.,Akutsu, M.,Wagner, S.A.,Beli, P.
p38-MK2 signaling axis regulates RNA metabolism after UV-light-induced DNA damage.
Nat Commun, 9:1017-1017, 2018

PubMed Abstract: Ultraviolet (UV) light radiation induces the formation of bulky photoproducts in the DNA that globally affect transcription and splicing. However, the signaling pathways and mechanisms that link UV-light-induced DNA damage to changes in RNA metabolism remain poorly understood. Here we employ quantitative phosphoproteomics and protein kinase inhibition to provide a systems view on protein phosphorylation patterns induced by UV light and uncover the dependencies of phosphorylation events on the canonical DNA damage signaling by ATM/ATR and the p38 MAP kinase pathway. We identify RNA-binding proteins as primary substrates and 14-3-3 as direct readers of p38-MK2-dependent phosphorylation induced by UV light. Mechanistically, we show that MK2 phosphorylates the RNA-binding subunit of the NELF complex NELFE on Serine 115. NELFE phosphorylation promotes the recruitment of 14-3-3 and rapid dissociation of the NELF complex from chromatin, which is accompanied by RNA polymerase II elongation.

PubMed: 29523821
DOI: 10.1038/s41467-018-03417-3

実験手法

X-RAY DIFFRACTION (2.7 Å)