Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 410, Issue 1, Pages 118-130Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2011.04.064
Keywords
translational control; energy metabolism; mass spectrometry; translational profiling; ribosome filter
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Funding
- National Institutes of Health [GM073732]
- Stanford ITI
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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.
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