MUL1 is an E3 ubiquitin-protein ligase with a RING finger domain that controls mitochondrial morphology, fragmentation and localization. E3 ubiquitin ligases accept the component ubiquitin from a donor E2 ubiquitin-conjugating directly transfer this ubiquitin to designated targeted substrates. The largest, proteome-wide and site-specific quantitative mapping dataset assessment of endogenous putative ubiquitylation sites and regulation was executed by Wagner’s group in Denmark1. Their compelling experiments also evaluated crosstalk between ubiquitylation and acetylation modifications using an MUL1 antibody. When overexpressed, MUL1 activates the JNK signal cascade and induces caspase-dependent apoptosis. MUL1 has also been shown to negatively regulate Akt kinase, suppressing cell proliferation and viability2.
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Western Blot: MUL1 Antibody
Cilenti’s group used the MUL1 antibody in immunoblotting experiments investigating the Omi/HtrA2 protease3. Omi/HtrA2 is a mitochondrial-specific serine protease with conflicting activity dependent on its subcellular localization – cytoplasmic release triggers apoptosis while inter-membrane space confinement produces a pro-survival activity. Cilenti’s used an MUL1 antibody in mutant mice to uncover a new stress-signaling pathway that starts in the mitochondria and could be a factor in motor neuron disease and premature aging.
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