MNK2 Inhibits eIF4G Activation Through a Pathway Involving Serine-Arginine–Rich Protein Kinase in Skeletal Muscle
Shou-Ih Hu, Mark Katz, Sherry Chin, Xiaoqing Qi, Joseph Cruz, Chikwendu Ibebunjo, Shanchuan Zhao, Amy Chen, David J. Glass*
*To whom correspondence should be addressed. E-mail:
This PDF file includes:
- Fig. S1. Densitometry quantification of the ratio of phospho/total eIF4G and eIF4E from Fig. 1A.
- Fig. S2. Densitometry quantification of the ratio of phospho/total eIF4G and p70S6K from Fig. 3A.
- Fig. S3. MNK2 overexpression partially inhibits global protein synthesis.
- Fig. S4. MNK2 and Pras40 compete for binding to Raptor.
- Fig. S5. MNK2 and SRPK1 interact with eIF4G.
- Fig. S6. Densitometry quantification of the ratio of phospho/total eIF4G in Fig. 5.
- Fig. S7. Expression of atrophy-associated genes and eIF4G phosphorylation status in gastrocnemius of a denervation-induced atrophy model.
- Fig. S8. Muscle mass in dexamethasone-induced and denervation-induced atrophy models.
- Fig. S9. Proposed negative role of MNK2 on protein translation through SRPK and TORC1.
- Table S1 legend
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Other Supplementary Material for this manuscript includes the following:
- Table S1 (Microsoft Excel format). Summary of primary mouse kinase panel siRNA screen.
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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).