Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the polyubiquitination of Mcl-1 and regulates apoptosis.
By Q. Zhong, Wenhua Gao, Fenghe Du, Xiaodong Wang. Cell, 2005
871 citations recorded by the source corpus.
Subfields: Molecular Biology, Oncology
View Paper: https://www.semanticscholar.org/paper/e83942aac7a9811d8134788659b0dbedaf44ca84
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Citations in the corpus
- A new pathway for mitochondrial quality control: mitochondrial‐derived vesicles (2014, background): “For example, the anti-apoptotic Bcl-2 family protein Mcl-1 is ubiquitinated by MULE during apoptosis, and its removal facilitates Bax activation and cell death (Warr et al, 2005; Zhong et al, 2005).”
- The BCL-2 protein family: opposing activities that mediate cell death (2008, background): “MULE has a BH3 domain and can loosely be considered to belong to the class of BH3-only proteins, which interact with and regulate other members of the BCL-2 famil”
- Control of mitochondrial apoptosis by the Bcl-2 family (2009, background): “Mcl-1 ubiquitylation ligase E3 (MULE) contains a BH3 domain that specifically binds Mcl-1, which leads to Mcl-1 ubiquitylation and degradation (Zhong et al., 2005).”
- mir-29 regulates Mcl-1 protein expression and apoptosis (2007, background): “Ubiquitination by the E3-ligase Mule leads to rapid degradation by the proteasome, and prevention of ubiquitination increases Mcl-1 levels and enhances protection (Zhong et al., 2005).”
- Life in the balance: how BH3-only proteins induce apoptosis. (2005, background): “However, Mcl-1 poly-ubiquitination can be catalyzed by the novel E3 ubiquitin ligase Mule/ARF-BP1, which also specifically binds Mcl-1 via a Bak-like BH3 domain [15 ].”
- The Bcl-2 apoptotic switch in cancer development and therapy (2007, background): “, 2005) and a BH3-containing E3 ubiquitin ligase called Mule (Zhong et al., 2005).”
- Glycogen synthase kinase-3 regulates mitochondrial outer membrane permeabilization and apoptosis by destabilization of MCL-1. (2006, background): “Among the evolutionary conserved MCL-1 lysine residues, Mule was shown to primarily mediate ubiquitinylation of lysines 136, 194, and 197 (Zhong et al., 2005).”
- p53 ubiquitination: Mdm2 and beyond. (2006, background): “Indeed, ARF-BP1/Mule/HectH9 has been shown to be important in regulating other proteins such as c-Myc and MCL-1 (Adhikary et al., 2005; Zhong et al., 2005), which mediate p53-independent functions.”
- The mitochondrial phosphatase PGAM5 functions at the convergence point of multiple necrotic death pathways. (2012, neutral): “Stable lines with inducible shRNA expression were established as previously described (Zhong et al., 2005).”
- The BH3 mimetic ABT-737 targets selective Bcl-2 proteins and efficiently induces apoptosis via Bak/Bax if Mcl-1 is neutralized. (2006, background): “Indeed, eventually it may prove feasible to enhance Mcl-1 degradation by augmenting the activity of the ubiquitin E3 ligase Mule (also known as ARF-BP1, Lasu, HectH9), which bears a BH3 domain targeting it to Mcl-1 (Zhong et al., 2005).”