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Data demonstrate a clear role for MAPL and mitochondrial SUMOylation in the activation of RIG-I (show DDX58 Proteins), a modification essential for the mitochondrial antiviral signaling response.
MULAN regulates NF-kappaappaB activation to protect cells from endoplasmic reticulum stress-induced apoptosis.
MUL1 ubiquitinates ULK1 (show ULK1 Proteins) and regulates selenite-induced mitophagy
Cigarette smoke-induced MUL1 elevation mediates Akt (show AKT1 Proteins) ubiquitination/degradation, potentially leading to pulmonary endothelial cell death and functional impairment.
Hades (MUL1)-mediated p73 (show TP73 Proteins) ubiquitination is a novel regulatory mechanism for the exonuclear function of p73 (show TP73 Proteins).
Activation of apoptosis triggers MAPL/MUL1-dependent SUMOylation of the fission GTPase (show RACGAP1 Proteins) Drp1 (show CRMP1 Proteins), a process requisite for cytochrome c (show CYCS Proteins) release.
The interaction of GABARAP (show GABARAP Proteins) with Mulan-Ube2E3 (show UBE2E3 Proteins) supports the role of Mulan as an important regulator of mitophagy.
MethyLight data demonstrated that C13orf18 and C1orf166 could not be considered as specific, sensitive and suitable prognostic biomarkers in cervical dysplasia related Papillomavirus Infections.
During stress-induced mitochondrial hyperfusion, MULAN forms a complex with TRAF2 (show TRAF2 Proteins) and modulates its ubiquitylation, signifying that TRAF2 (show TRAF2 Proteins) may serve as an ubiquitylated transmitter of NF-kappaB (show NFKB1 Proteins) signaling in this pathway
MUL1 is a novel regulator of the RIG-I (show DDX58 Proteins)-like receptor-dependent antiviral response, that otherwise functions to limit inflammation.
Our results indicate that strict maternal transmission of mitochondria relies on mitophagy and uncover a collaboration between MUL1 and PARKIN (show PARK2 Proteins) in this process.
Inactivation of Omi/HtrA2 (show HTRA2 Proteins) protease leads to the deregulation of mitochondrial Mulan E3 ubiquitin ligase and increased mitophagy.
These results suggest that Tnrip-1 is a testis-specific (show AIF1 Proteins) and GCNF (show NR6A1 Proteins)-interacting protein which may be involved in the modulation of GCNF (show NR6A1 Proteins)-mediated gene transcription in spermatogenic cells within the testis.
E3 ubiquitin-protein ligase that plays a role in the control of mitochondrial morphology. Promotes mitochondrial fragmentation and influences mitochondrial localization. Inhibits cell growth. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates (By similarity).
E3 SUMO-protein ligase MUL1
, E3 ubiquitin ligase
, E3 ubiquitin-protein ligase MUL1
, growth inhibition and death E3 ligase
, mitochondria-anchored protein ligase
, mitochondrial E3 ubiquitin ligase 1
, mitochondrial ubiquitin ligase activator of NF-kB
, mitochondrial ubiquitin ligase activator of NFKB 1
, mitochondrial-anchored protein ligase
, putative NF-kappa-B-activating protein 266
, ring finger protein 218
, mitochondrial ubiquitin ligase activator of NFKB 1-like
, mitochondrial ubiquitin ligase activator of nfkb 1
, E3 ubiquitin-protein ligase mul1