Gotowe bibliografie tematyczne / Ubiquitin kinase PINK1

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Gotowa bibliografia na temat „Ubiquitin kinase PINK1”

Autor: Grafiati

Data publikacji: 3 czerwca 2025

Data aktualizacji: 31 lipca 2025

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Artykuły w czasopismach na temat "Ubiquitin kinase PINK1"

Zheng, Xinde, and Tony Hunter. "Pink1, the first ubiquitin kinase." EMBO Journal 33, no. 15 (2014): 1621–23. http://dx.doi.org/10.15252/embj.201489185.

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Kane, Lesley A., Michael Lazarou, Adam I. Fogel, et al. "PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase activity." Journal of Cell Biology 205, no. 2 (2014): 143–53. http://dx.doi.org/10.1083/jcb.201402104.

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PINK1 kinase activates the E3 ubiquitin ligase Parkin to induce selective autophagy of damaged mitochondria. However, it has been unclear how PINK1 activates and recruits Parkin to mitochondria. Although PINK1 phosphorylates Parkin, other PINK1 substrates appear to activate Parkin, as the mutation of all serine and threonine residues conserved between Drosophila and human, including Parkin S65, did not wholly impair Parkin translocation to mitochondria. Using mass spectrometry, we discovered that endogenous PINK1 phosphorylated ubiquitin at serine 65, homologous to the site phosphorylated by P

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Kazlauskaite, Agne, Chandana Kondapalli, Robert Gourlay, et al. "Parkin is activated by PINK1-dependent phosphorylation of ubiquitin at Ser65." Biochemical Journal 460, no. 1 (2014): 127–41. http://dx.doi.org/10.1042/bj20140334.

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We describe a novel and unexpected mechanism by which PINK1 protein kinase activates Parkin E3 ligase. We show that PINK1 phosphorylates ubiquitin at Ser65 and that phosphorylated ubiquitin acts as a direct activator of Parkin.

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Aguirre, Jacob D., Karen M. Dunkerley, Pascal Mercier, and Gary S. Shaw. "Structure of phosphorylated UBL domain and insights into PINK1-orchestrated parkin activation." Proceedings of the National Academy of Sciences 114, no. 2 (2016): 298–303. http://dx.doi.org/10.1073/pnas.1613040114.

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Mutations in PARK2 and PARK6 genes are responsible for the majority of hereditary Parkinson’s disease cases. These genes encode the E3 ubiquitin ligase parkin and the protein kinase PTEN-induced kinase 1 (PINK1), respectively. Together, parkin and PINK1 regulate the mitophagy pathway, which recycles damaged mitochondria following oxidative stress. Native parkin is inactive and exists in an autoinhibited state mediated by its ubiquitin-like (UBL) domain. PINK1 phosphorylation of serine 65 in parkin’s UBL and serine 65 of ubiquitin fully activate ubiquitin ligase activity; however, a structural

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Lazarou, Michael, Derek P. Narendra, Seok Min Jin, Ephrem Tekle, Soojay Banerjee, and Richard J. Youle. "PINK1 drives Parkin self-association and HECT-like E3 activity upstream of mitochondrial binding." Journal of Cell Biology 200, no. 2 (2013): 163–72. http://dx.doi.org/10.1083/jcb.201210111.

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Genetic studies indicate that the mitochondrial kinase PINK1 and the RING-between-RING E3 ubiquitin ligase Parkin function in the same pathway. In concurrence, mechanistic studies show that PINK1 can recruit Parkin from the cytosol to the mitochondria, increase the ubiquitination activity of Parkin, and induce Parkin-mediated mitophagy. Here, we used a cell-free assay to recapitulate PINK1-dependent activation of Parkin ubiquitination of a validated mitochondrial substrate, mitofusin 1. We show that PINK1 activated the formation of a Parkin–ubiquitin thioester intermediate, a hallmark of HECT

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Broadway, Benjamin J., Paige K. Boneski, Jenny M. Bredenberg, et al. "Systematic Functional Analysis of PINK1 and PRKN Coding Variants." Cells 11, no. 15 (2022): 2426. http://dx.doi.org/10.3390/cells11152426.

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Loss of either PINK1 or PRKN causes an early onset Parkinson’s disease (PD) phenotype. Functionally, PINK1 and PRKN work together to mediate stress-activated mitochondrial quality control. Upon mitochondrial damage, PINK1, a ubiquitin kinase and PRKN, a ubiquitin ligase, decorate damaged organelles with phosphorylated ubiquitin for sequestration and degradation in lysosomes, a process known as mitophagy. While several genetic mutations are established to result in loss of mitophagy function, many others have not been extensively characterized and are of unknown significance. Here, we analyzed

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Di Rita, Anthea, Teresa Maiorino, Krenare Bruqi, Floriana Volpicelli, Gian Carlo Bellenchi, and Flavie Strappazzon. "miR-218 Inhibits Mitochondrial Clearance by Targeting PRKN E3 Ubiquitin Ligase." International Journal of Molecular Sciences 21, no. 1 (2020): 355. http://dx.doi.org/10.3390/ijms21010355.

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The selective elimination of dysfunctional mitochondria through mitophagy is crucial for preserving mitochondrial quality and cellular homeostasis. The most described mitophagy pathway is regulated by a positive ubiquitylation feedback loop in which the PINK1 (PTEN induced kinase 1) kinase phosphorylates both ubiquitin and the E3 ubiquitin ligase PRKN (Parkin RBR E3 ubiquitin ligase), also known as PARKIN. This event recruits PRKN to the mitochondria, thus amplifying ubiquitylation signal. Here we report that miR-218 targets PRKN and negatively regulates PINK1/PRKN-mediated mitophagy. Overexpr

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Shaw, Gary S. "Switching on ubiquitylation by phosphorylating a ubiquitous activator." Biochemical Journal 460, no. 3 (2014): e1-e3. http://dx.doi.org/10.1042/bj20140459.

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The dysfunction of the E3 ubiquitin ligase Parkin is a key contributor to the development of early-onset Parkinson's disease. Parkin is responsible for the labelling of outer mitochondrial membrane proteins with the small modifier protein ubiquitin in response to oxidative stress. This ubiquitylation signals the clearance of the damaged mitochondria to preserve overall cell health. Recent structural and biochemical experiments have shown that native Parkin exists in an autoinhibited state that must be activated in order to unmask its full ubiquitylation potential. In a recent article in the Bi

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Torres-Odio, Sylvia, Jana Key, Hans-Hermann Hoepken, et al. "Progression of pathology in PINK1-deficient mouse brain from splicing via ubiquitination, ER stress, and mitophagy changes to neuroinflammation." Journal of Neuroinflammation 14, no. 1 (2017): 154. https://doi.org/10.1186/s12974-017-0928-0.

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<strong>Background: </strong>PINK1 deficiency causes the autosomal recessive PARK6 variant of Parkinson's disease. PINK1 activates ubiquitin by phosphorylation and cooperates with the downstream ubiquitin ligase PARKIN, to exert quality control and control autophagic degradation of mitochondria and of misfolded proteins in all cell types.<strong>Methods: </strong>Global transcriptome profiling of mouse brain and neuron cultures were assessed in protein-protein interaction diagrams and by pathway enrichment algorithms. Validation by quantitative reverse transcriptase polymerase chain reaction a

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Lazarou, Michael, Danielle A. Sliter, Lesley A. Kane, et al. "The ubiquitin kinase PINK1 recruits autophagy receptors to induce mitophagy." Nature 524, no. 7565 (2015): 309–14. http://dx.doi.org/10.1038/nature14893.

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Rozprawy doktorskie na temat "Ubiquitin kinase PINK1"

Schubert, Alexander Fabian. "Mechanism of PINK1-mediated ubiquitin phosphorylation." Thesis, University of Cambridge, 2018. https://www.repository.cam.ac.uk/handle/1810/277271.

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Ubiquitin phosphorylation by PINK1 (PTEN-induced Putative Kinase 1) is crucial for mitochondrial quality control and loss or mutation of PINK1 can lead to autosomal recessive juvenile parkinsonism (AR-JP). PINK1 is an unusual kinase, as it is characterised by three unique insertions in its kinase N lobe and a C-terminal region after the kinase domain. Despite great effort, a structure of PINK1 could not be determined and the molecular mechanism of ubiquitin phosphorylation and the effect of the PINK1 AR-JP patient mutations remained elusive. The versatile modifier ubiquitin (Ub) is also an unu

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