The ubiquitin kinase PINK1 recruits autophagy receptors to induce mitophagy
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...PentaKO cells were unable to eliminate mitochondria following activation of the PINK1–Parkin pathway and rescue experiments revealed that NDP52 andOPTN are required yet redundant for mitophagy [53]....
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...Several lines of evidence indicate that PINK1 stabilization on the OMM leads to phosphorylation of pre-existing ubiquitin molecules at the mitochondrial surface: mitochondrially targeted phosphomimetic ubiquitin is able to recruit and activate Parkin [52]; ubiquitin phosphorylation is detected without Parkin [49]; and low levels of mitophagy persist even in the absence of Parkin [53]....
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...Mitophagy is inhibited in NDP52–OPTN double knockout cell lines [53,62], and knockdown of OPTN alone has been reported to impede mitophagy [63] at early time points [64]....
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...Mitochondrial damage induces TBK1 activation as evidenced by TBK1 phosphorylation at Ser172, which is dependent on both Parkin and PINK1 expression [53] and ubiquitin binding of receptor proteins [62]....
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...TBK1 phosphorylation of OPTN on Ser473 and Ser513 increases OPTN’s affinity for ubiquitin chains [62,65] and phospho-Ub chains [53,65]....
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...…to allow recognition by sequestosome 1 (SQSTM1, best known as p62) (to a limited extent), optineurin (OPTN), calcium binding and coiled-coil domain 2 (CALCOCO2; best known as NDP52), and LC3 (Wong & Holzbaur, 2014; Heo et al, 2015; Lazarou et al, 2015; Moore & Holzbaur, 2016; Wei et al, 2017)....
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References
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