Optineurin is an autophagy receptor for damaged mitochondria in parkin-mediated mitophagy that is disrupted by an ALS-linked mutation

By Y. Wong, E. Holzbaur. Proceedings of the National Academy of Sciences of the United States of America, 2014

772 citations recorded by the source corpus.

Subfields: Epidemiology, Neurology, Physiology

View Paper: https://www.semanticscholar.org/paper/09af23e443e70ca6000bc3c6d971b085d2b8a03b

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Epidemiology

In Neurology

In Physiology

Citations in the corpus

Phosphorylation of OPTN by TBK1 enhances its binding to Ub chains and promotes selective autophagy of damaged mitochondria (2016, background): “Increased activation of TBK1 upon Parkin overexpression is presumably connected to its interplay with OPTN, because stable recruitment of OPTN to mitochondria also depends on the presence of Parkin (28).”
Exome sequencing in amyotrophic lateral sclerosis identifies risk genes and pathways (2015, positive): “Additionally, OPTN also functions in the autophagic turnover of damaged mitochondria via the PARKIN ubiquitin ligase pathway (35).”
Deciphering the Molecular Signals of PINK1/Parkin Mitophagy. (2016, background): “ALS-associated mutations in Optineurin that disrupt ubiquitin binding (E478G and Q398X) are defective in mitophagy [42–44] while the E50K mutation linked with glaucoma has only a moderate mitophagy defect [43].”
Molecular definitions of autophagy and related processes (2017, positive): “This enables the association of the PI3P-binding proteins DFCP1 and WIPI2 (Polson et al , 2010), the formation of ATG12-ATG5:ATG16L1 complexes, and consequent local LC3 lipidation (Dooley et al , 2014).”
Atg8 family LC3/GABARAP proteins are crucial for autophagosome–lysosome fusion but not autophagosome formation during PINK1/Parkin mitophagy and starvation (2016, background): “Autophagosome formation on the mitochondrial surface is mediated by the mitophagy receptors optineurin and NDP52 (Wong and Holzbaur, 2014; Heo et al., 2015; Lazarou et al., 2015), which promote recruitment of the autophagy-initiating kinase ULK1 (Lazarou et al.”
The PINK1-PARKIN mitochondrial ubiquitylation pathway drives a program of TBK1 activation and recruitment of OPTN and NDP52 to promote mitophagy (2015, background): “First, OPTN was found to promote mitophagy in HeLa cells (Wong and Holzbaur, 2014), as well as restrict Salmonella infection in tissue culture cells, where its phosphorylation on S177 by TBK1 is thought to promote association with ATG8 proteins (Wild et al.”
Autophagy-Dependent Ferroptosis: Machinery and Regulation (2020, positive): “In addition to its role in the bulk degradation process, MAP1LC3-II also interacts with cargo receptors (e.g., sequestosome 1 [SQSTM1/p62], calcium-binding and coiled-coil domain 2 [CALCOCO2/ NDP52], and optineurin [OPTN]) to regulate the process of selective forms of autophagy.”
Autophagy and Neurodegeneration: Pathogenic Mechanisms and Therapeutic Opportunities. (2017, positive): “Following either loss of huntingtin, or expression of the mutant protein, a decrease autophagosome transport and subsequent inhibition of substrate degradation was observed (Wong and Holzbaur, 2014a).”