Research

Hormonal

The E3 ubiquitin ligase MAFbx (Atrogin-1) directly binds to MyoD via a conserved LXXLL motif interaction, leading to MyoD ubiquitination and proteasomal degradation, which suppresses myogenic differentiation.

This research identifies MAFbx as a key enzyme that degrades MyoD, a master regulator of muscle growth. High levels of MAFbx, often seen during muscle atrophy (caused by fasting, aging, or disuse), lead to the loss of MyoD and inhibit muscle formation. Preserving muscle mass may involve mechanisms that regulate or inhibit MAFbx activity.

GoodSupportsHIGH confidence
Here we report that MyoD interacts with Atrogin-1/MAFbx (MAFbx), a striated muscle-specific E3 ubiquitin ligase dramatically up-regulated in atrophying muscle. A core LXXLL motif sequence in MyoD is necessary for binding to MAFbx... Overexpression of MAFbx suppresses MyoD-induced differentiation and inhibits myotube formation.
Lionel Tintignac et al. · Journal of Biological Chemistry · 2004

Why this rating

High-quality biochemical evidence (yeast two-hybrid, co-IP, in vitro ubiquitination, in vivo models) with clear mechanistic validation via mutations.

Source

Degradation of MyoD Mediated by the SCF (MAFbx) Ubiquitin Ligase

Lionel Tintignac et al. · Journal of Biological Chemistry · 2004

DOI 10.1074/jbc.m411346200

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DOI resolved against Crossref · corpus check 2026-06-10

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