期刊
CELL
卷 169, 期 6, 页码 1051-+出版社
CELL PRESS
DOI: 10.1016/j.cell.2017.05.022
关键词
-
资金
- New York Stem Cell Foundation [NYSCF-R-I36]
- NIH [7DP2OD008509, R21HD086730, 1F30CA189514-01]
- Alfred P. Sloan Research Fellowship
- Mallinckrodt Foundation Award
- Pew Scholars Award
- Stanford Medical Scientist Training Program
- Paul and Daisy Soros Fellowships for New Americans and Stanford Medical Scientist Training Program
- Benchmark Stanford Graduate Fellowship
- [P50-HG007735]
- [R01-HG004361]
- [R01-ES023168]
During eukaryotic evolution, ribosomes have considerably increased in size, forming a surface-exposed ribosomal RNA (rRNA) shell of unknown function, which may create an interface for yet uncharacterized interacting proteins. To investigate such protein interactions, we establish a ribosome affinity purification method that unexpectedly identifies hundreds of ribosome-associated proteins (RAPs) from categories including metabolism and cell cycle, as well as RNA-and protein-modifying enzymes that functionally diversify mammalian ribosomes. By further characterizing RAPs, we discover the presence of ufmylation, a metazoan-specific post-translational modification (PTM), on ribosomes and define its direct substrates. Moreover, we show that the metabolic enzyme, pyruvate kinase muscle (PKM), interacts with sub-pools of endoplasmic reticulum (ER)-associated ribosomes, exerting a non-canonical function as an RNA-binding protein in the translation of ER-destined mRNAs. Therefore, RAPs interconnect one of life's most ancient molecular machines with diverse cellular processes, providing an additional layer of regulatory potential to protein expression.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据