MNK2 Inhibits eIF4G Activation Through a Pathway Involving Serine-Arginine–Rich Protein Kinase in Skeletal Muscle-Reference-Cited by-同舟云学术

MNK2 Inhibits eIF4G Activation Through a Pathway Involving Serine-Arginine–Rich Protein Kinase in Skeletal Muscle

Published:2012-02-14 Issue:211 Volume:5 Page:
ISSN:1945-0877
Container-title:Science Signaling
language:en
Short-container-title:Sci. Signal.

Author:

Hu Shou-Ih¹,Katz Mark¹,Chin Sherry¹,Qi Xiaoqing¹,Cruz Joseph¹,Ibebunjo Chikwendu¹,Zhao Shanchuan¹,Chen Amy¹,Glass David J.¹

Affiliation:

1. Novartis Institutes for Biomedical Research, 100 Technology Square, Cambridge, MA 02139, USA.

Abstract

In muscle, the kinase-dependent and -independent functions of MNK2 inhibit the protein translation protein eIF4G under conditions that promote atrophy.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference49 articles.

1. The E3 Ligase MuRF1 Degrades Myosin Heavy Chain Protein in Dexamethasone-Treated Skeletal Muscle

2. During muscle atrophy, thick, but not thin, filament components are degraded by MuRF1-dependent ubiquitylation

3. MAFbx/Atrogin-1 Controls the Activity of the Initiation Factor eIF3-f in Skeletal Muscle Atrophy by Targeting Multiple C-terminal Lysines

4. The initiation factor eIF3-f is a major target for Atrogin1/MAFbx function in skeletal muscle atrophy

5. Mediation of IGF-1-induced skeletal myotube hypertrophy by PI(3)K/Akt/mTOR and PI(3)K/Akt/GSK3 pathways

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