Molecular interaction between parkin and PINK1 in mammalian neuronal cells

Um, Ji Won; Stichel-Gunkel, Christine C.; Lübbert, Hermann; Lee, Gwang; Chung, Kwang Chul

doi:10.1016/j.mcn.2008.12.010

Cited by 61 publications

(48 citation statements)

References 48 publications

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“…3A and B). Partial colocalization of wild-type PINK1 with parkin has been previously reported in cells overexpressing both PINK1 and parkin; however, the association with mitochondria was not examined [15]. Also, parkin colocalization with PINK1 in aggregated mitochondria has been previously reported [8].…”

Section: Mitochondrial Elimination Is Accomplished By Overexpression mentioning

confidence: 92%

PINK1 is recruited to mitochondria with parkin and associates with LC3 in mitophagy

et al. 2010

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Edited by Jesus AvilaKeywords: PTEN-induced putative kinase 1 Parkin Mitophagy Autophagy Parkinson's disease a b s t r a c t Mutations in PTEN-induced putative kinase 1 (PINK1) cause recessive form of Parkinson's disease (PD). PINK1 acts upstream of parkin, regulating mitochondrial integrity and functions. Here, we show that PINK1 in combination with parkin results in the perinuclear mitochondrial aggregation followed by their elimination. This elimination is reduced in cells expressing PINK1 mutants with wild-type parkin. Although wild-type PINK1 localizes in aggregated mitochondria, PINK1 mutants localization remains diffuse and mitochondrial elimination is not observed. This phenomenon is not observed in autophagy-deficient cells. These results suggest that mitophagy controlled by the PINK1/parkin pathway might be associated with PD pathogenesis. Structured summary:MINT-7557195: PINK1 (uniprotkb:Q9BXM7) physically interacts (MI:0915) with LC3 (uniprotkb:Q9GZQ8) by anti tag coimmunoprecipitation (MI:0007) MINT-7557109: LC3 (uniprotkb:Q9GZQ8) and PINK1

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Section: Mitochondrial Elimination Is Accomplished By Overexpression mentioning

confidence: 92%

PINK1 is recruited to mitochondria with parkin and associates with LC3 in mitophagy

et al. 2010

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“…The ubiquitin E3 ligase parkin can bind selectively to damaged mitochondria and participates in the engulfment of damaged mitochondria in preautophagosomal structures (Narendra et al 2008). PINK1-mediated phosphorylation of Parkin is a requirement for this translocation, and the interaction of PINK1 and Parkin has mutual effects on their solubility (Kim et al 2008;Shiba et al 2009;Um et al 2009;Xiong et al 2009). Consequently Parkin can rescue mitochondrial dysfunction after knockout of PINK1 in D. melanogaster (Park et al 2006;Yang et al 2006) and also in HeLa cells (Exner et al 2007).…”

Section: Role Of Pink1 In Stress Responsementioning

confidence: 99%

The mitochondrial kinase PINK1, stress response and Parkinson’s disease

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Gispert

Ricciardi

et al. 2009

J Bioenerg Biomembr

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“…17 Meanwhile, several studies have found similar PINK1-stabilizing effects of Parkin as well as converse Parkin-destabilizing effects of PINK1 under steady-state conditions and particularly upon cellular stress. 17,[19][20][21][22] The latter may result from a reduction of Parkin solubility 19,20 and/or from an augmented proteasomal degradation of Parkin in the presence of PINK1. 21,22 Although accumulating biochemical data support a delicate interaction between PINK1 and Parkin and thereby underscore the importance of the physical binding of both, several aspects await closer examination.…”

Section: Introductionmentioning

confidence: 99%

“…It has now been demonstrated by several groups that exogenous 12,[16][17][18][19][20][21] as well as endogenous 9 PINK1 and Parkin indeed physically interact with each other. While the respective binding sites have not been exactly identified so far, it is noteworthy that Parkin robustly binds to all three isoforms of PINK1.…”

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confidence: 99%