Proteomic Analysis of Ribosomes: Translational Control of mRNA Populations by Glycogen Synthase GYS1

被引:29
作者
Fuchs, Gabriele [1 ]
Diges, Camille [1 ]
Kohlstaedt, Lori A. [2 ]
Wehner, Karen A. [1 ]
Sarnow, Peter [1 ]
机构
[1] Stanford Univ, Sch Med, Dept Microbiol & Immunol, Stanford, CA 94305 USA
[2] Univ Calif Berkeley, Prote Mass Spectrometry Lab, Berkeley, CA 94720 USA
基金
美国国家卫生研究院;
关键词
translational control; energy metabolism; mass spectrometry; translational profiling; ribosome filter; P40/LAMININ RECEPTOR PRECURSOR; MASS-SPECTROMETRIC ANALYSIS; PROTEINS; SUBUNITS; GENE; PHOSPHORYLATION; IDENTIFICATION; FIBROBLASTS; SENSITIVITY; INITIATION;
D O I
10.1016/j.jmb.2011.04.064
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Ribosomes exist as a heterogenous pool of macromolecular complexes composed of ribosomal RNA molecules, ribosomal proteins, and numerous associated "nonribosomal" proteins. To identify nonribosomal proteins that may modulate ribosome activity, we examined the composition of translationally active and inactive ribosomes using a proteomic multidimensional protein identification technology. Notably, the phosphorylated isoform of glycogen synthase, glycogen synthase 1 (GYS1), was preferentially associated with elongating ribosomes. Depletion of GYS1 affected the translation of a subset of cellular mRNAs, some of which encode proteins that modulate protein biosynthesis. These findings argue that GYS1 abundance, by virtue of its ribosomal association, provides a feedback loop between the energy state of the cells and the translation machinery. (C) 2011 Elsevier Ltd. All rights reserved.
引用
收藏
页码:118 / 130
页数:13
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