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Sci. Signal., 14 February 2012
[DOI: 10.1126/scisignal.2002466]

Supplementary Materials for:

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: david.glass{at}novartis.com

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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Technical Details

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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.

[Download Table S1]

Technical Details

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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).

© 2012 American Association for the Advancement of Science


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