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December 11, 2008Journal of Biological ChemistryOpen Access

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

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Population

In cellulo and in vivo models of starvation-induced skeletal muscle atrophy

Design

Preclinical

Authors

ACAlfredo CsibiUniversité Paris-SudMLMarie Pierre LeibovitchDynamique Musculaire et MétabolismeKCKaren CornilleUniversity of Basel

Discussion

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Overview

Supports eIF3-f lysine targeting to counter muscle atrophy in models; leaves open translation to human therapies.

Structured PICO

P
Population
In cellulo and in vivo models of starvation-induced skeletal muscle atrophy
I
Intervention
Mutation of six lysine residues within the C-terminal domain of eIF3-f (mutant K(5-10)R)
O
Outcome
Polyubiquitination, proteasomal degradation, and protection against starvation-induced muscle atrophysurrogate

The six C-terminal lysines of eIF3-f are essential for MAFbx-directed polyubiquitination and degradation, and their mutation protects against skeletal muscle atrophy.

Cite This Study

Csibi et al. (2008) studied this question.

synapsesocial.com/papers/6a87bf0920275dc7c70151c2https://doi.org/10.1074/jbc.m807641200
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Also Consider

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  1. 1Mapping of Functional Domains in Eukaryotic Protein Synthesis Initiation Factor 4G (eIF4G) with Picornaviral Proteases1995 · 558 citations
  2. 2Insulin-like Growth Factor-1 (IGF-1) Inversely Regulates Atrophy-induced Genes via the Phosphatidylinositol 3-Kinase/Akt/Mammalian Target of Rapamycin (PI3K/Akt/mTOR) Pathway2004 · 529 citations
  3. 3The ubiquitin-proteasome pathway: The complexity and myriad functions of proteins death1998 · 519 citations
  4. 4eIF3-f function in skeletal muscles: To stand at the crossroads of atrophy and hypertrophy2008 · 29 citations
  5. 5What do we really know about the ubiquitin-proteasome pathway in muscle atrophy?2001 · 401 citations