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

Kawajiri, Sumihiro; Saiki, Sachio; Sato, Shigeto; Sato, Fumiaki; Hatano, Taku; Eguchi, Hiroto; Hattori, Nobutaka

doi:10.1016/j.febslet.2010.02.016

Cited by 222 publications

(186 citation statements)

References 20 publications

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“…Later studies have supported Narendra's findings showing that PINK1 acts upstream from Parkin, and that both proteins are recruited to depolarized mitochondria (Kim et al, 2008;Kawajiri et al, 2010;Matsuda et al, 2010;Vives-Bauza et al, 2010). The DJ-1 protein, already known by its antioxidant, chaperone-like and transcriptional modulator functions, has been recently proposed to act in parallel with PINK1 and…”

Section: Linking Oxidative Stress and Mitochondrial Dynamics In Pd Amentioning

confidence: 72%

Mitochondrial respiratory chain dysfunction: Implications in neurodegeneration

Morán

Moreno-Lastres

Marín-Buera

et al. 2012

Free Radical Biology and Medicine

144

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For decades mitochondria have been considered static round shaped organelles in charge of energy production. On the contrary, they are highly dynamic cellular components that undergo continuous cycles of fusion and fission influenced, for instance, by oxidative stress, cellular energy requirements, or the cell cycle state. New important functions beyond energy production have been attributed to mitochondria, such as the regulation of cell survival due to their role in the modulation of apoptosis, autophagy and aging. Primary mitochondrial diseases due to mutations in genes involved in these new mitochondrial functions, and the implication of mitochondrial dysfunction in multifactorial human pathologies like cancer, Alzheimer's and Parkinson's diseases, or diabetes has been demonstrated. Therefore, mitochondria are set at a central point of the equilibrium between health and disease, and a better understanding of mitochondrial functions will open new fields to explore the role of these mitochondrial pathways in human pathologies. The present review will dissect the relationships between the activity and assembly defects of the mitochondrial respiratory chain, oxidative damage, and alterations in mitochondrial dynamics, with special focus at their implications in neurodegeneration.

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Section: Linking Oxidative Stress and Mitochondrial Dynamics In Pd Amentioning

confidence: 72%

Mitochondrial respiratory chain dysfunction: Implications in neurodegeneration

Morán

Moreno-Lastres

Marín-Buera

et al. 2012

Free Radical Biology and Medicine

144

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“…As outlined above, many studies in the field of mitophagy involve a determination of colocalization between mitochondrial labels and markers for autophagy (for example MAP1LC3 19,21,23,29,30 ) or other salient proteins such as PARK2 30,31 or PINK1 30 The recruitment of mitochondria has also been analyzed through colocalization of other autophagy markers such as Atg8 or GABARAPL1 with Atg32 26,27 or BNIP3L, 15 respectively. Quantification of the extent to which markers colocalize provides a numerical index that can be subjected to statistical analysis.…”

Section: Image Analysis and Quantification Of Mitophagymentioning

confidence: 99%

“…The second family are the GABA A receptor-associated proteins (GABARAP) which has four members: the first is GABARAP, the second member is GABARAPL1 (GABA(A) receptor-associated protein like 1)/ATG8L/GEC1, the third member is GABARAPL2 (GABA(A) receptor-associated protein like 2)/GATE-16/GEF2, with the final member GABARAPL3 (GABA(A) receptor-associated protein like 3). 28 Examples where mitochondria have been labeled along with MAP1LC3 as either a fluorescent protein (FP) chimera 19,21,23,29 or by using antibodies raised against MAP1LC3 30 are noted. MAP1LC3 reporters can also be combined with many other mitochondrial/mitophagy fluorescent markers, including TMRM, 21 mitochondrial-targeted RFP, 19 PARK2 as an FP chimera, 30,31 PINK1 (Flag epitope-tagged PINK1), 30 and MitoTracker ® dyes.…”

Section: Monitoring Mitophagy Through Colocalization Of Mitochondrialmentioning

confidence: 99%

“…28 Examples where mitochondria have been labeled along with MAP1LC3 as either a fluorescent protein (FP) chimera 19,21,23,29 or by using antibodies raised against MAP1LC3 30 are noted. MAP1LC3 reporters can also be combined with many other mitochondrial/mitophagy fluorescent markers, including TMRM, 21 mitochondrial-targeted RFP, 19 PARK2 as an FP chimera, 30,31 PINK1 (Flag epitope-tagged PINK1), 30 and MitoTracker ® dyes. 29 MAP1LC3 colocalization with mitochondrial markers provides a reliable indication that the mitochondria in question are destined for autophagic degradation and as as will be discussed later, colocalization of mitochondria with lysosomal markers indicates successful trafficking to the lysosome itself.…”

Section: Monitoring Mitophagy Through Colocalization Of Mitochondrialmentioning

confidence: 99%

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Tools and techniques to measure mitophagy using fluorescence microscopy

et al. 2013

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“…In the present study, we observed Parkin aggregation in the neural cells of embryos from diabetic dams, suggesting that an impaired Parkin-mediated UPS may be involved in diabetic embryopathy. PARKIN interacts with PTEN-induced putative kinase 1 (PINK1) on the mitochondrial membrane (48,49). The action of the PARKIN-PINK1 complex is to regulate mitochondrial morphogenesis and remove damaged mitochondria through a form of ALS (50,51).…”

Section: Discussionmentioning

confidence: 99%

Formation of neurodegenerative aggresome and death-inducing signaling complex in maternal diabetes-induced neural tube defects

Zhao

Cao

Reece

2017

Proc. Natl. Acad. Sci. U.S.A.

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Diabetes mellitus in early pregnancy increases the risk in infants of birth defects, such as neural tube defects (NTDs), known as diabetic embryopathy. NTDs are associated with hyperglycemia-induced protein misfolding and Caspase-8–induced programmed cell death. The present study shows that misfolded proteins are ubiquitinylated, suggesting that ubiquitin-proteasomal degradation is impaired. Misfolded proteins form aggregates containing ubiquitin-binding protein p62, suggesting that autophagic-lysosomal clearance is insufficient. Additionally, these aggregates contain the neurodegenerative disease-associated proteins α-Synuclein, Parkin, and Huntingtin (Htt). Aggregation of Htt may lead to formation of a death-inducing signaling complex of Hip1, Hippi, and Caspase-8. Treatment with chemical chaperones, such as sodium 4-phenylbutyrate (PBA), reduces protein aggregation in neural stem cells in vitro and in embryos in vivo. Furthermore, treatment with PBA in vivo decreases NTD rate in the embryos of diabetic mice, as well as Caspase-8 activation and cell death. Enhancing protein folding could be a potential interventional approach to preventing embryonic malformations in diabetic pregnancies.

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

Cited by 222 publications

References 20 publications

Mitochondrial respiratory chain dysfunction: Implications in neurodegeneration

Mitochondrial respiratory chain dysfunction: Implications in neurodegeneration

Tools and techniques to measure mitophagy using fluorescence microscopy

Formation of neurodegenerative aggresome and death-inducing signaling complex in maternal diabetes-induced neural tube defects

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