Please use this identifier to cite or link to this item: https://scholarbank.nus.edu.sg/handle/10635/149304
Title: PTEN-L IS A NOVEL PROTEIN PHOSPHATASE FOR UBIQUITIN DEPHOSPHORYLATION TO INHIBIT PINK1-PARKIN-MEDIATED MITOPHAGY
Authors: WANG LIMING
Keywords: mitophagy, phosphatase, ubiquitin, PTEN-L, Parkin, PINK1
Issue Date: 17-Aug-2018
Citation: WANG LIMING (2018-08-17). PTEN-L IS A NOVEL PROTEIN PHOSPHATASE FOR UBIQUITIN DEPHOSPHORYLATION TO INHIBIT PINK1-PARKIN-MEDIATED MITOPHAGY. ScholarBank@NUS Repository.
Abstract: Mitophagy, a selective form of autophagy for removal of damaged mitochondria and defective mitophagy, is well known to be implicated in the pathogenesis of neurodegenerative disorders, in particular Parkinson’s disease. PTEN-induced kinase protein 1 (PINK1)-mediated phosphorylation of ubiquitin plays a critical role in the onset of mitophagy. Phosphatase and tensin homolog (PTEN)-long (PTEN-L) is a newly identified isoform of PTEN, with addition of 173 amino acids to its N-terminal. In this study, we report a novel function of PTEN-L in the regulation of mitophagy. PTEN-L localizes on the outer mitochondrial membrane and inhibits Parkin mitochondrial translocation, its E3 ligase activity and phosphorylation induced by mitochondrial damaging agents. Moreover, PTEN-L reduces phospho-ubiquitin (pSer65-Ub) and in vitro phosphatase assay confirms that PTEN-L dephosphorylates ubiquitin via its protein phosphatase activity independent of its lipid phosphatase function. Thus, our findings demonstrate that PTEN-L is a novel protein phosphatase for ubiquitin in suppression of mitophagy.
URI: http://scholarbank.nus.edu.sg/handle/10635/149304
Appears in Collections:Ph.D Theses (Open)

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