Sci. Signal., 14 February 2012
Limiting Muscle MassSkeletal muscle mass changes in response to activity, the availability of nutrients, and pathologic loss of muscle mass are associated with long-term bed rest, cachexia-inducing diseases, and starvation. Hu et al. used overexpression, knockout, and knockdown studies to show that the kinase MNK2 had a negative regulatory role on proteins involved in protein synthesis under atrophy-promoting conditions. This was unexpected because MNK2 is also part of a eukaryotic translation initiation complex and is one of the two isoforms capable of phosphorylating a component of that complex on a site associated with promotion of protein synthesis. The negative regulatory effects on protein synthesis machinery appeared to involve a kinase-independent interaction with mTOR, a master regulator of protein synthesis, and a kinase-dependent regulation of another kinase, SRPK, which had not been previously implicated in regulation of protein synthesis.
Citation: S.-I. Hu, M. Katz, S. Chin, X. Qi, J. Cruz, C. Ibebunjo, S. Zhao, A. Chen, D. J. Glass, MNK2 Inhibits eIF4G Activation Through a Pathway Involving Serine-Arginine–Rich Protein Kinase in Skeletal Muscle. Sci. Signal. 5, ra14 (2012).
The editors suggest the following Related Resources on Science sites:
In Science Signaling
THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882