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Artykuły w czasopismach na temat „Ubiquitin kinase PINK1”

Autor: Grafiati

Data publikacji: 3 czerwca 2025

Data aktualizacji: 31 lipca 2025

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1

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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3

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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4

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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5

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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6

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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8

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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9

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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10

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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Erpapazoglou, Zoi, and Olga Corti. "The endoplasmic reticulum/mitochondria interface: a subcellular platform for the orchestration of the functions of the PINK1–Parkin pathway?" Biochemical Society Transactions 43, no. 2 (2015): 297–301. http://dx.doi.org/10.1042/bst20150008.

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Mitochondrial dysfunction is a hallmark of both idiopathic and familial Parkinson's disease (PD). Mutations in the PARK2 and PARK6 genes, coding for the cytosolic E3 ubiquitin protein ligase Parkin and the mitochondrial serine/threonine kinase PINK1 [phosphatase and tensin homologue (PTEN)-induced putative kinase 1], lead to clinically similar early-onset Parkinsonian syndromes. PINK1 and Parkin cooperate within a conserved pathway to preserve mitochondrial quality through the regulation of a variety of processes, including mitochondrial dynamics, transport, bioenergetics, biogenesis and turno

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Torii, Satoru, Shuya Kasai, Tatsushi Yoshida, Ken-ichi Yasumoto, and Shigeomi Shimizu. "Mitochondrial E3 Ubiquitin Ligase Parkin: Relationships with Other Causal Proteins in Familial Parkinson’s Disease and Its Substrate-Involved Mouse Experimental Models." International Journal of Molecular Sciences 21, no. 4 (2020): 1202. http://dx.doi.org/10.3390/ijms21041202.

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Parkinson’s disease (PD) is a common neurodegenerative disorder. Recent identification of genes linked to familial forms of PD has revealed that post-translational modifications, such as phosphorylation and ubiquitination of proteins, are key factors in disease pathogenesis. In PD, E3 ubiquitin ligase Parkin and the serine/threonine-protein kinase PTEN-induced kinase 1 (PINK1) mediate the mitophagy pathway for mitochondrial quality control via phosphorylation and ubiquitination of their substrates. In this review, we first focus on well-characterized PINK1 phosphorylation motifs. Second, we de

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13

Heo, Jin-Mi, Nathan J. Harper, Joao A. Paulo, et al. "Integrated proteogenetic analysis reveals the landscape of a mitochondrial-autophagosome synapse during PARK2-dependent mitophagy." Science Advances 5, no. 11 (2019): eaay4624. http://dx.doi.org/10.1126/sciadv.aay4624.

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The PINK1 protein kinase activates the PARK2 ubiquitin ligase to promote mitochondrial ubiquitylation and recruitment of ubiquitin-binding mitophagy receptors typified by OPTN and TAX1BP1. Here, we combine proximity biotinylation of OPTN and TAX1BP1 with CRISPR-Cas9–based screens for mitophagic flux to develop a spatial proteogenetic map of PARK2-dependent mitophagy. Proximity labeling of OPTN allowed visualization of a “mitochondrial-autophagosome synapse” upon mitochondrial depolarization. Proximity proteomics of OPTN and TAX1BP1 revealed numerous proteins at the synapse, including both PARK

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14

Moore, D. J. "Parkin: a multifaceted ubiquitin ligase." Biochemical Society Transactions 34, no. 5 (2006): 749–53. http://dx.doi.org/10.1042/bst0340749.

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Mutations in the parkin gene are a common cause of autosomal recessive early-onset parkinsonism. Parkin functions as an E3 ubiquitin ligase where it can polyubiquitinate a number of its protein substrates, thus targeting them for degradation by the 26 S proteasomal complex. Recent studies have demonstrated that alternative modes of parkin-mediated ubiquitination may serve other non-degradative regulatory roles. In addition, parkin appears to function as a multipurpose neuroprotectant in a number of toxic paradigms. Coupled with these observations, parkin may integrate other gene products assoc

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15

Whiten, Daniel R., Dezerae Cox, and Carolyn M. Sue. "PINK1 signalling in neurodegenerative disease." Essays in Biochemistry 65, no. 7 (2021): 913–23. http://dx.doi.org/10.1042/ebc20210036.

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Abstract PTEN-induced kinase 1 (PINK1) impacts cell health and human pathology through diverse pathways. The strict processing of full-length PINK1 on the outer mitochondrial membrane populates a cytoplasmic pool of cleaved PINK1 (cPINK1) that is constitutively degraded. However, despite rapid proteasomal clearance, cPINK1 still appears to exert quality control influence over the neuronal protein homeostasis network, including protein synthesis and degradation machineries. The cytoplasmic concentration and activity of this molecule is therefore a powerful sensor that coordinates aspects of mit

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Ordureau, Alban, Jin-Mi Heo, David M. Duda, et al. "Defining roles of PARKIN and ubiquitin phosphorylation by PINK1 in mitochondrial quality control using a ubiquitin replacement strategy." Proceedings of the National Academy of Sciences 112, no. 21 (2015): 6637–42. http://dx.doi.org/10.1073/pnas.1506593112.

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The PTEN-induced putative kinase protein 1 (PINK1) and ubiquitin (UB) ligase PARKIN direct damaged mitochondria for mitophagy. PINK1 promotes PARKIN recruitment to the mitochondrial outer membrane (MOM) for ubiquitylation of MOM proteins with canonical and noncanonical UB chains. PINK1 phosphorylates both Ser65 (S65) in the UB-like domain of PARKIN and the conserved Ser in UB itself, but the temporal sequence and relative importance of these events during PARKIN activation and mitochondria quality control remain poorly understood. Using “UBS65A-replacement,” we find that PARKIN phosphorylation

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17

Wang, Y., K. G. Jia, H. J. Xing, et al. "Interaction of SENP6 with PINK1 promotes temozolomide resistance in neuroglioma cells via inducing the mitophagy." Молекулярная биология 58, no. 1 (2024): 126–29. http://dx.doi.org/10.31857/s0026898424010112.

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Temozolomide resistance is a major cause of recurrence and poor prognosis in neuroglioma. Recently, growing evidence has suggested that mitophagy is involved in drug resistance in various tumor types. However, the role and molecular mechanisms of mitophagy in temozolomide resistance in glioma remain unclear. In this study, mitophagy levels in temozolomide-resistant and -sensitive cell lines were evaluated. The mechanisms underlying the regulation of mitophagy were explored through RNA sequencing, and the roles of differentially expressed genes in mitophagy and temozolomide resistance were inve

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18

Matsuda, Noriyuki, Shigeto Sato, Kahori Shiba, et al. "PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy." Journal of Cell Biology 189, no. 2 (2010): 211–21. http://dx.doi.org/10.1083/jcb.200910140.

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Parkinson's disease (PD) is a prevalent neurodegenerative disorder. Recent identification of genes linked to familial forms of PD such as Parkin and PINK1 (PTEN-induced putative kinase 1) has revealed that ubiquitylation and mitochondrial integrity are key factors in disease pathogenesis. However, the exact mechanism underlying the functional interplay between Parkin-catalyzed ubiquitylation and PINK1-regulated mitochondrial quality control remains an enigma. In this study, we show that PINK1 is rapidly and constitutively degraded under steady-state conditions in a mitochondrial membrane poten

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Kazlauskaite, Agne, Van Kelly, Clare Johnson, et al. "Phosphorylation of Parkin at Serine65 is essential for activation: elaboration of a Miro1 substrate-based assay of Parkin E3 ligase activity." Open Biology 4, no. 3 (2014): 130213. http://dx.doi.org/10.1098/rsob.130213.

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Mutations in PINK1 and Parkin are associated with early-onset Parkinson's disease. We recently discovered that PINK1 phosphorylates Parkin at serine65 (Ser 65 ) within its Ubl domain, leading to its activation in a substrate-free activity assay. We now demonstrate the critical requirement of Ser 65 phosphorylation for substrate ubiquitylation through elaboration of a novel in vitro E3 ligase activity assay using full-length untagged Parkin and its putative substrate, the mitochondrial GTPase Miro1. We observe that Parkin efficiently ubiquitylates Miro1 at highly conserved lysine residues, 153,

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20

Imai, Yuzuru. "Mitochondrial Regulation by PINK1-Parkin Signaling." ISRN Cell Biology 2012 (December 17, 2012): 1–15. http://dx.doi.org/10.5402/2012/926160.

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Two genes responsible for the juvenile Parkinson’s disease (PD), PINK1 and Parkin, have been implicated in mitochondrial quality control. The inactivation of PINK1, which encodes a mitochondrial kinase, leads to age-dependent mitochondrial degeneration in Drosophila. The phenotype is closely associated with the impairment of mitochondrial respiratory chain activity and defects in mitochondrial dynamics. Drosophila genetic studies have further revealed that PINK1 is an upstream regulator of Parkin and is involved in the mitochondrial dynamics and motility. A series of cell biological studies ha

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Shlevkov, Evgeny, Tal Kramer, Jason Schapansky, Matthew J. LaVoie, and Thomas L. Schwarz. "Miro phosphorylation sites regulate Parkin recruitment and mitochondrial motility." Proceedings of the National Academy of Sciences 113, no. 41 (2016): E6097—E6106. http://dx.doi.org/10.1073/pnas.1612283113.

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The PTEN-induced putative kinase 1 (PINK1)/Parkin pathway can tag damaged mitochondria and trigger their degradation by mitophagy. Before the onset of mitophagy, the pathway blocks mitochondrial motility by causing Miro degradation. PINK1 activates Parkin by phosphorylating both Parkin and ubiquitin. PINK1, however, has other mitochondrial substrates, including Miro (also called RhoT1 and -2), although the significance of those substrates is less clear. We show that mimicking PINK1 phosphorylation of Miro on S156 promoted the interaction of Parkin with Miro, stimulated Miro ubiquitination and

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Scott, Helen L., Nicola Buckner, Francesc Fernandez-Albert, et al. "A dual druggable genome-wide siRNA and compound library screening approach identifies modulators of parkin recruitment to mitochondria." Journal of Biological Chemistry 295, no. 10 (2020): 3285–300. http://dx.doi.org/10.1074/jbc.ra119.009699.

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Genetic and biochemical evidence points to an association between mitochondrial dysfunction and Parkinson's disease (PD). PD-associated mutations in several genes have been identified and include those encoding PTEN-induced putative kinase 1 (PINK1) and parkin. To identify genes, pathways, and pharmacological targets that modulate the clearance of damaged or old mitochondria (mitophagy), here we developed a high-content imaging-based assay of parkin recruitment to mitochondria and screened both a druggable genome-wide siRNA library and a small neuroactive compound library. We used a multiparam

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Sauvé, Véronique, and Kalle Gehring. "Deciphering the activation of the E3 ubiquitin ligase parkin." Acta Crystallographica Section A Foundations and Advances 70, a1 (2014): C836. http://dx.doi.org/10.1107/s2053273314091633.

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Parkin is an E3 ubiquitin ligase responsible for some autosomal recessive forms of Parkinson's disease. Even though parkin is a RING-type E3 ligase, it uses a hybrid RING/HECT mechanism for its activity. The crystal structures of full-length and the RING0-RING1-In-Between-RING-RING2 module of parkin reveal a conformation of parkin in which its E2 binding site is too far from its catalytic cysteine for the transfer of ubiquitin [1]. Many intramolecular interactions occur between the different RING domains, as well as with a repressor element, which, with RING0, are unique to parkin. Mutations o

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Youn, Dong Hyuk, Bong Jun Kim, Eun Pyo Hong, and Jin Pyeong Jeon. "Bioinformatics Analysis of Autophagy and Mitophagy Markers Associated with Delayed Cerebral Ischemia Following Subarachnoid Hemorrhage." Journal of Korean Neurosurgical Society 65, no. 2 (2022): 236–44. http://dx.doi.org/10.3340/jkns.2021.0169.

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Objective : To evaluate the interactions among differentially expressed autophagy and mitophagy markers in subarachnoid hemorrhage (SAH) patients with delayed cerebral ischemia (DCI).Methods : The expression data of autophagy and mitophagy-related makers in the cerebrospinal fluid (CSF) cells was analyzed by real-time reverse transcription-polymerase chain reaction and Western blotting. The markers included death-associated protein kinase (DAPK)-1, BCL2 interacting protein 3 like (BNIP3L), Bcl-1 antagonist X, phosphatase and tensin homolog-induced kinase (PINK), Unc-51 like autophagy activatin

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Walden, Helen, and Miratul M. K. Muqit. "Ubiquitin and Parkinson's disease through the looking glass of genetics." Biochemical Journal 474, no. 9 (2017): 1439–51. http://dx.doi.org/10.1042/bcj20160498.

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Biochemical alterations found in the brains of Parkinson's disease (PD) patients indicate that cellular stress is a major driver of dopaminergic neuronal loss. Oxidative stress, mitochondrial dysfunction, and ER stress lead to impairment of the homeostatic regulation of protein quality control pathways with a consequent increase in protein misfolding and aggregation and failure of the protein degradation machinery. Ubiquitin signalling plays a central role in protein quality control; however, prior to genetic advances, the detailed mechanisms of how impairment in the ubiquitin system was linke

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Salazar, Celia, Paula Ruiz-Hincapie, and Lina Ruiz. "The Interplay among PINK1/PARKIN/Dj-1 Network during Mitochondrial Quality Control in Cancer Biology: Protein Interaction Analysis." Cells 7, no. 10 (2018): 154. http://dx.doi.org/10.3390/cells7100154.

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PARKIN (E3 ubiquitin ligase PARK2), PINK1 (PTEN induced kinase 1) and DJ-1 (PARK7) are proteins involved in autosomal recessive parkinsonism, and carcinogenic processes. In damaged mitochondria, PINK1’s importing into the inner mitochondrial membrane is prevented, PARKIN presents a partial mitochondrial localization at the outer mitochondrial membrane and DJ-1 relocates to mitochondria when oxidative stress increases. Depletion of these proteins result in abnormal mitochondrial morphology. PINK1, PARKIN, and DJ-1 participate in mitochondrial remodeling and actively regulate mitochondrial quali

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Huang, Shiyuan, Xiaona Wang, Jiale Yu, et al. "LonP1 regulates mitochondrial network remodeling through the PINK1/Parkin pathway during myoblast differentiation." American Journal of Physiology-Cell Physiology 319, no. 6 (2020): C1020—C1028. http://dx.doi.org/10.1152/ajpcell.00589.2019.

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Myoblast differentiation is a crucial process for myogenesis. Mitochondria function as an energy-providing machine that is critical to this process, and mitochondrial dysfunction can prevent myoblasts from fusing into myotubes. However, the molecular mechanisms underlying the dynamic regulation of mitochondrial networks remain poorly understood. In the present study, we found that the PTEN induced kinase 1 (PINK1)/Parkin (an E3 ubiquitin-protein ligase) pathway is activated at the early stage of myoblast differentiation. Moreover, downregulation of mitofusin 2 (Mfn2) and increased dynamin-rela

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Caulfield, Thomas R., Fabienne C. Fiesel, and Wolfdieter Springer. "Activation of the E3 ubiquitin ligase Parkin." Biochemical Society Transactions 43, no. 2 (2015): 269–74. http://dx.doi.org/10.1042/bst20140321.

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The PINK1 (phosphatase and tensin homologue-induced putative kinase 1)/Parkin-dependent mitochondrial quality control pathway mediates the clearance of damaged organelles, but appears to be disrupted in Parkinson's disease (PD) [Springer and Kahle (2011) Autophagy 7, 266–278]. Upon mitochondrial stress, PINK1 activates the E3 ubiquitin (Ub) ligase Parkin through phosphorylation of the Ub-like (UBL) domain of Parkin and of the small modifier Ub itself at a conserved residue [Sauvé and Gehring (2014) Cell Res. 24, 1025–1026]. Recently resolved partial crystal structures of Parkin showed a ‘close

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Bader, Verian, and Konstanze F. Winklhofer. "PINK1 and Parkin: team players in stress-induced mitophagy." Biological Chemistry 401, no. 6-7 (2020): 891–99. http://dx.doi.org/10.1515/hsz-2020-0135.

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AbstractMitochondria are highly vulnerable organelles based on their complex biogenesis, entailing dependence on nuclear gene expression and efficient import strategies. They are implicated in a wide spectrum of vital cellular functions, including oxidative phosphorylation, iron-sulfur cluster synthesis, regulation of calcium homeostasis, and apoptosis. Moreover, damaged mitochondria can release mitochondrial components, such as mtDNA or cardiolipin, which are sensed as danger-associated molecular patterns and trigger innate immune signaling. Thus, dysfunctional mitochondria pose a thread not

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Heo, J. M., A. Ordureau, S. Swarup, et al. "RAB7A phosphorylation by TBK1 promotes mitophagy via the PINK-PARKIN pathway." Science Advances 4, no. 11 (2018): eaav0443. http://dx.doi.org/10.1126/sciadv.aav0443.

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Removal of damaged mitochondria is orchestrated by a pathway involving the PINK1 kinase and the PARKIN ubiquitin ligase. Ubiquitin chains assembled by PARKIN on the mitochondrial outer membrane recruit autophagy cargo receptors in complexes with TBK1 protein kinase. While TBK1 is known to phosphorylate cargo receptors to promote ubiquitin binding, it is unknown whether TBK1 phosphorylates other proteins to promote mitophagy. Using global quantitative proteomics, we identified S72 in RAB7A, a RAB previously linked with mitophagy, as a dynamic target of TBK1 upon mitochondrial depolarization. TB

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Panicker, Nikhil, Valina L. Dawson, and Ted M. Dawson. "Activation mechanisms of the E3 ubiquitin ligase parkin." Biochemical Journal 474, no. 18 (2017): 3075–86. http://dx.doi.org/10.1042/bcj20170476.

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Monogenetic, familial forms of Parkinson's disease (PD) only account for 5–10% of the total number of PD cases, but analysis of the genes involved therein is invaluable to understanding PD-associated neurodegenerative signaling. One such gene, parkin, encodes a 465 amino acid E3 ubiquitin ligase. Of late, there has been considerable interest in the role of parkin signaling in PD and in identifying its putative substrates, as well as the elucidation of the mechanisms through which parkin itself is activated. Its dysfunction underlies both inherited and idiopathic PD-associated neurodegeneration

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Richter, Benjamin, Danielle A. Sliter, Lina Herhaus, et al. "Phosphorylation of OPTN by TBK1 enhances its binding to Ub chains and promotes selective autophagy of damaged mitochondria." Proceedings of the National Academy of Sciences 113, no. 15 (2016): 4039–44. http://dx.doi.org/10.1073/pnas.1523926113.

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Selective autophagy of damaged mitochondria requires autophagy receptors optineurin (OPTN), NDP52 (CALCOCO2), TAX1BP1, and p62 (SQSTM1) linking ubiquitinated cargo to autophagic membranes. By using quantitative proteomics, we show that Tank-binding kinase 1 (TBK1) phosphorylates all four receptors on several autophagy-relevant sites, including the ubiquitin- and LC3-binding domains of OPTN and p62/SQSTM1 as well as the SKICH domains of NDP52 and TAX1BP1. Constitutive interaction of TBK1 with OPTN and the ability of OPTN to bind to ubiquitin chains are essential for TBK1 recruitment and kinase

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Ham, Su Jin, Soo Young Lee, Saera Song, Ju-Ryung Chung, Sekyu Choi, and Jongkyeong Chung. "Interaction between RING1 (R1) and the Ubiquitin-like (UBL) Domains Is Critical for the Regulation of Parkin Activity." Journal of Biological Chemistry 291, no. 4 (2015): 1803–16. http://dx.doi.org/10.1074/jbc.m115.687319.

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Parkin is an E3 ligase that contains a ubiquitin-like (UBL) domain in the N terminus and an R1-in-between-ring-RING2 motif in the C terminus. We showed that the UBL domain specifically interacts with the R1 domain and negatively regulates Parkin E3 ligase activity, Parkin-dependent mitophagy, and Parkin translocation to the mitochondria. The binding between the UBL domain and the R1 domain was suppressed by carbonyl cyanide m-chlorophenyl hydrazone treatment or by expression of PTEN-induced putative kinase 1 (PINK1), an upstream kinase that phosphorylates Parkin at the Ser-65 residue of the UB

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Hu, Xinchao, Chengyuan Mao, Liyuan Fan, et al. "Modeling Parkinson’s Disease Using Induced Pluripotent Stem Cells." Stem Cells International 2020 (March 12, 2020): 1–15. http://dx.doi.org/10.1155/2020/1061470.

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Parkinson’s disease (PD) is the second most common neurodegenerative disease. The molecular mechanisms of PD at the cellular level involve oxidative stress, mitochondrial dysfunction, autophagy, axonal transport, and neuroinflammation. Induced pluripotent stem cells (iPSCs) with patient-specific genetic background are capable of directed differentiation into dopaminergic neurons. Cell models based on iPSCs are powerful tools for studying the molecular mechanisms of PD. The iPSCs used for PD studies were mainly from patients carrying mutations in synuclein alpha (SNCA), leucine-rich repeat kina

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Ham, Su Jin, Daewon Lee, Wen Jun Xu, et al. "Loss of UCHL1 rescues the defects related to Parkinson’s disease by suppressing glycolysis." Science Advances 7, no. 28 (2021): eabg4574. http://dx.doi.org/10.1126/sciadv.abg4574.

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The role of ubiquitin carboxyl-terminal hydrolase L1 (UCHL1; also called PARK5) in the pathogenesis of Parkinson’s disease (PD) has been controversial. Here, we find that the loss of UCHL1 destabilizes pyruvate kinase (PKM) and mitigates the PD-related phenotypes induced by PTEN-induced kinase 1 (PINK1) or Parkin loss-of-function mutations in Drosophila and mammalian cells. In UCHL1 knockout cells, cellular pyruvate production and ATP levels are diminished, and the activity of AMP–activated protein kinase (AMPK) is highly induced. Consequently, the activated AMPK promotes the mitophagy mediate

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Potting, Christoph, Christophe Crochemore, Francesca Moretti, et al. "Genome-wide CRISPR screen for PARKIN regulators reveals transcriptional repression as a determinant of mitophagy." Proceedings of the National Academy of Sciences 115, no. 2 (2017): E180—E189. http://dx.doi.org/10.1073/pnas.1711023115.

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PARKIN, an E3 ligase mutated in familial Parkinson’s disease, promotes mitophagy by ubiquitinating mitochondrial proteins for efficient engagement of the autophagy machinery. Specifically, PARKIN-synthesized ubiquitin chains represent targets for the PINK1 kinase generating phosphoS65-ubiquitin (pUb), which constitutes the mitophagy signal. Physiological regulation of PARKIN abundance, however, and the impact on pUb accumulation are poorly understood. Using cells designed to discover physiological regulators of PARKIN abundance, we performed a pooled genome-wide CRISPR/Cas9 knockout screen. Te

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Nezich, Catherine L., Chunxin Wang, Adam I. Fogel, and Richard J. Youle. "MiT/TFE transcription factors are activated during mitophagy downstream of Parkin and Atg5." Journal of Cell Biology 210, no. 3 (2015): 435–50. http://dx.doi.org/10.1083/jcb.201501002.

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The kinase PINK1 and ubiquitin ligase Parkin can regulate the selective elimination of damaged mitochondria through autophagy (mitophagy). Because of the demand on lysosomal function by mitophagy, we investigated a role for the transcription factor EB (TFEB), a master regulator of lysosomal biogenesis, in this process. We show that during mitophagy TFEB translocates to the nucleus and displays transcriptional activity in a PINK1- and Parkin-dependent manner. MITF and TFE3, homologues of TFEB belonging to the same microphthalmia/transcription factor E (MiT/TFE) family, are similarly regulated d

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Mauri, Sofia, Greta Bernardo, Aitor Martinez, et al. "USP8 Down-Regulation Promotes Parkin-Independent Mitophagy in the Drosophila Brain and in Human Neurons." Cells 12, no. 8 (2023): 1143. http://dx.doi.org/10.3390/cells12081143.

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Stress-induced mitophagy, a tightly regulated process that targets dysfunctional mitochondria for autophagy-dependent degradation, mainly relies on two proteins, PINK1 and Parkin, which genes are mutated in some forms of familiar Parkinson’s Disease (PD). Upon mitochondrial damage, the protein kinase PINK1 accumulates on the organelle surface where it controls the recruitment of the E3-ubiquitin ligase Parkin. On mitochondria, Parkin ubiquitinates a subset of mitochondrial-resident proteins located on the outer mitochondrial membrane, leading to the recruitment of downstream cytosolic autophag

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Kim, Heejeong, Byeong Tak Jeon, Isaac M. Kim, et al. "Sestrin2 Phosphorylation by ULK1 Induces Autophagic Degradation of Mitochondria Damaged by Copper-Induced Oxidative Stress." International Journal of Molecular Sciences 21, no. 17 (2020): 6130. http://dx.doi.org/10.3390/ijms21176130.

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Selective autolysosomal degradation of damaged mitochondria, also called mitophagy, is an indispensable process for maintaining integrity and homeostasis of mitochondria. One well-established mechanism mediating selective removal of mitochondria under relatively mild mitochondria-depolarizing stress is PINK1-Parkin-mediated or ubiquitin-dependent mitophagy. However, additional mechanisms such as LC3-mediated or ubiquitin-independent mitophagy induction by heavy environmental stress exist and remain poorly understood. The present study unravels a novel role of stress-inducible protein Sestrin2

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Huang, Chusheng, Lipeng Li, Hailong Deng, et al. "Exploring miR-3148’s impact on Krüppel-like factor 6-driven mitophagy and apoptosis in myocardial ischemic injury." Cytojournal 22 (February 14, 2025): 19. https://doi.org/10.25259/cytojournal_209_2024.

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Objective Myocardial infarction (MI) is a leading cause of death worldwide, accounting for millions of fatalities annually. The injury and repair of cardiomyocytes are closely associated with the changes in gene expression. MicroRNAs could serve as a potential target for MI treatment. This work aims to investigate the role of miR-3148 in mitochondrial dynamics during acute MI (AMI) with a specific focus on its regulatory mechanisms in mitophagy and apoptosis, which could reveal potential therapeutic targets for AMI treatment. Material and Methods MiR-3148 levels in patients with AMI and experi

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Bednarczyk, Martyna, Małgorzata Muc-Wierzgoń, Sylwia Dzięgielewska-Gęsiak, and Dariusz Waniczek. "Relationship between the Ubiquitin–Proteasome System and Autophagy in Colorectal Cancer Tissue." Biomedicines 11, no. 11 (2023): 3011. http://dx.doi.org/10.3390/biomedicines11113011.

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Background: Dysregulation of the autophagy process via ubiquitin is associated with the occurrence of a number of diseases, including cancer. The present study analyzed the changes in the transcriptional activity of autophagy-related genes and the ubiquitination process (UPS) in colorectal cancer tissue. (2) Methods: The process of measuring the transcriptional activity of autophagy-related genes was analyzed by comparing colorectal cancer samples from four clinical stages I-IV (CS I-IV) of adenocarcinoma to the control (C). The transcriptional activity of genes associated with the UPS pathway

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Hung, Chien-Min, Portia S. Lombardo, Nazma Malik, et al. "AMPK/ULK1-mediated phosphorylation of Parkin ACT domain mediates an early step in mitophagy." Science Advances 7, no. 15 (2021): eabg4544. http://dx.doi.org/10.1126/sciadv.abg4544.

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The serine/threonine kinase ULK1 mediates autophagy initiation in response to various cellular stresses, and genetic deletion of ULK1 leads to accumulation of damaged mitochondria. Here we identify Parkin, the core ubiquitin ligase in mitophagy, and PARK2 gene product mutated in familial Parkinson’s disease, as a ULK1 substrate. Recent studies uncovered a nine residue (“ACT”) domain important for Parkin activation, and we demonstrate that AMPK-dependent ULK1 rapidly phosphorylates conserved serine108 in the ACT domain in response to mitochondrial stress. Phosphorylation of Parkin Ser108 occurs

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Sun, Zhe, Zicheng Ma, Wandi Cao, et al. "Calcium-mediated mitochondrial fission and mitophagy drive glycolysis to facilitate arterivirus proliferation." PLOS Pathogens 21, no. 1 (2025): e1012872. https://doi.org/10.1371/journal.ppat.1012872.

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Mitochondria, recognized as the “powerhouse” of cells, play a vital role in generating cellular energy through dynamic processes such as fission and fusion. Viruses have evolved mechanisms to hijack mitochondrial function for their survival and proliferation. Here, we report that infection with the swine arterivirus porcine reproductive and respiratory syndrome virus (PRRSV), manipulates mitochondria calcium ions (Ca2+) to induce mitochondrial fission and mitophagy, thereby reprogramming cellular energy metabolism to facilitate its own replication. Mechanistically, PRRSV-induced mitochondrial

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Yoo, Lang, and Kwang Chul Chung. "The ubiquitin E3 ligase CHIP promotes proteasomal degradation of the serine/threonine protein kinase PINK1 during staurosporine-induced cell death." Journal of Biological Chemistry 293, no. 4 (2017): 1286–97. http://dx.doi.org/10.1074/jbc.m117.803890.

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Islam, Naeyma N., Caleb A. Weber, Matt Coban, et al. "In Silico Investigation of Parkin-Activating Mutations Using Simulations and Network Modeling." Biomolecules 14, no. 3 (2024): 365. http://dx.doi.org/10.3390/biom14030365.

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Complete loss-of-function mutations in the PRKN gene are a major cause of early-onset Parkinson’s disease (PD). PRKN encodes the Parkin protein, an E3 ubiquitin ligase that works in conjunction with the ubiquitin kinase PINK1 in a distinct quality control pathway to tag damaged mitochondria for autophagic clearance, i.e., mitophagy. According to previous structural investigations, Parkin protein is typically kept in an inactive conformation via several intramolecular, auto-inhibitory interactions. Here, we performed molecular dynamics simulations (MDS) to provide insights into conformational c

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Dunkerley, Karen M., Anne C. Rintala-Dempsey, Giulia Salzano, et al. "Distinct phosphorylation signals drive acceptor versus free ubiquitin chain targeting by parkin." Biochemical Journal 479, no. 6 (2022): 751–66. http://dx.doi.org/10.1042/bcj20210741.

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The RBR E3 ligase parkin is recruited to the outer mitochondrial membrane (OMM) during oxidative stress where it becomes activated and ubiquitinates numerous proteins. Parkin activation involves binding of a phosphorylated ubiquitin (pUb), followed by phosphorylation of the Ubl domain in parkin, both mediated by the OMM kinase, PINK1. How an OMM protein is selected for ubiquitination is unclear. Parkin targeted OMM proteins have little structural or sequence similarity, with the commonality between substrates being proximity to the OMM. Here, we used chimeric proteins, tagged with ubiquitin (U

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Moore, Andrew S., and Erika L. F. Holzbaur. "Dynamic recruitment and activation of ALS-associated TBK1 with its target optineurin are required for efficient mitophagy." Proceedings of the National Academy of Sciences 113, no. 24 (2016): E3349—E3358. http://dx.doi.org/10.1073/pnas.1523810113.

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Mitochondria play an essential role in maintaining cellular homeostasis. The removal of damaged or depolarized mitochondria occurs via mitophagy, in which damaged mitochondria are targeted for degradation via ubiquitination induced by PTEN-induced putative kinase 1 (PINK1) and Parkin. Mitophagy receptors, including optineurin (OPTN), nuclear dot 52 kDa protein (NDP52), and Tax1-binding protein 1 (TAX1BP1), are recruited to mitochondria via ubiquitin binding and mediate autophagic engulfment through their association with microtubule-associated protein light chain 3 (LC3). Here, we use live-cel

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Andrew, D. Waddell, Ojha Hina, Agarwal Shalini, et al. "Regulation of Human PINK1 ubiquitin kinase by Serine167, Serine228 and Cysteine412 phosphorylation." April 10, 2023. https://doi.org/10.5281/zenodo.7813605.

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Loss-of-function mutations in the human PINK1 kinase (<em>h</em>PINK1) are causative of early-onset Parkinson’s disease (PD). Activation of <em>h</em>PINK1 induces phosphorylated ubiquitin to initiate removal of damaged mitochondria by autophagy. Previously we solved the structure of the insect PINK1 orthologue, <em>Tribolium castaneum </em>PINK1, and showed that autophosphorylation of Ser205 was critical for ubiquitin interaction and phosphorylation (Kumar, Tamjar, Waddell et al., 2017). In this advance, we report new findings on the regulation of <em>h</em>PINK1 by phosphorylation. We

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Gan, Zhong Yan, Sylvie Callegari, Thanh N. Nguyen, et al. "Interaction of PINK1 with nucleotides and kinetin." Science Advances 10, no. 3 (2024). http://dx.doi.org/10.1126/sciadv.adj7408.

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The ubiquitin kinase PINK1 accumulates on damaged mitochondria to trigger mitophagy, and PINK1 loss-of-function mutations cause early onset Parkinson’s disease. Nucleotide analogs such as kinetin triphosphate (KTP) were reported to enhance PINK1 activity and may represent a therapeutic strategy for the treatment of Parkinson’s disease. Here, we investigate the interaction of PINK1 with nucleotides, including KTP. We establish a cryo-EM platform exploiting the dodecamer assembly of Pediculus humanus corporis ( Ph ) PINK1 and determine PINK1 structures bound to AMP-PNP and ADP, revealing conform

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Singh, Pawan K., Shalini Agarwal, Ilaria Volpi, et al. "Kinome screening identifies integrated stress response kinase EIF2AK1/HRI as a negative regulator of PINK1 mitophagy signaling." Science Advances 11, no. 19 (2025). https://doi.org/10.1126/sciadv.adn2528.

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Loss-of-function mutations in the PINK1 kinase lead to early-onset Parkinson’s disease (PD). PINK1 is activated by mitochondrial damage to phosphorylate ubiquitin and Parkin, triggering mitophagy. PINK1 also indirectly phosphorylates Rab GTPases, such as Rab8A. Using an siRNA library targeting human Ser/Thr kinases in HeLa cells, we identified EIF2AK1 [heme-regulated inhibitor (HRI) kinase], a branch of the integrated stress response (ISR), as a negative regulator of PINK1. EIF2AK1 knockdown enhances mitochondrial depolarization–induced PINK1 stabilization and phosphorylation of ubiquitin and

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