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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 04 Jul 2015.

Parkinson protein 2, E3 ubiquitin protein ligase

E3 ubiquitin ligase, Parkin, PARK2
The precise function of this gene is unknown; however, the encoded protein is a component of a multiprotein E3 ubiquitin ligase complex that mediates the targeting of substrate proteins for proteasomal degradation. Mutations in this gene are known to cause Parkinson disease and autosomal recessive juvenile Parkinson disease. Alternative splicing of this gene produces multiple transcript variants encoding distinct isoforms. Additional splice variants of this gene have been described but currently lack transcript support. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: PINK1, Ubiquitin, CAN, AGE, DJ-1
Papers on E3 ubiquitin ligase
Activation of autophagic flux against xenoestrogen Bisphenol-A induced hippocampal neurodegeneration via AMPK/mTOR pathways.
New
Chaturvedi et al., India. In J Biol Chem, 02 Aug 2015
BPA mediated neurotoxicity also resulted in mitochondrial loss, bioenergetic deficits, and increased Parkin mitochondrial translocation, suggesting enhanced mitophagy.
Exercise modulates liver cellular and mitochondrial proteins related to quality control signalling.
New
Ascensão et al., Porto, Portugal. In Life Sci, 29 Jul 2015
Liver mitochondrial alterations were evaluated by semi-quantification of proteins involved in oxidative stress (SIRT3, p66shc, p66(Ser36)), biogenesis (citrate synthase, PGC-1α and mtTFA), dynamics (MFN1, OPA1 and DRP1) and auto(mito)phagy (Beclin-1, Bcl-2, LC3II/LC3I, p62, Parkin and PINK) signalling.
Mitochondrial dysfunction and Parkinson disease: a Parkin-AMPK alliance in neuroprotection.
New
Lim et al., Singapore, Singapore. In Ann N Y Acad Sci, 29 Jul 2015
Particularly strong support for this came from the recent demonstration that parkin, a familial PD-linked gene, is a critical regulator of mitochondrial quality control.
Binding to serine 65-phosphorylated ubiquitin primes Parkin for optimal PINK1-dependent phosphorylation and activation.
New
Muqit et al., Dundee, United Kingdom. In Embo Rep, 25 Jul 2015
We and other groups have reported that PINK1 activates Parkin E3 ligase activity both directly via phosphorylation of Parkin serine 65 (Ser(65))-which lies within its ubiquitin-like domain (Ubl)-and indirectly through phosphorylation of ubiquitin at Ser(65).
Physical exercise improves brain cortex and cerebellum mitochondrial bioenergetics and alters apoptotic, dynamic and auto(mito)phagy markers.
New
Ascensão et al., Porto, Portugal. In Neuroscience, 23 Jul 2015
Mitochondrial dynamics (Mfn1/2, OPA1 and DRP1) and auto(mito)phagy (LC3II, Beclin1, Pink1, Parkin, p62)-related proteins were also measured by Western blotting.
AMPK Activation of Muscle Autophagy Prevents Fasting-Induced Hypoglycemia and Myopathy during Aging.
New
Impact
Steinberg et al., Hamilton, Canada. In Cell Metab, 02 Jul 2015
Consistent with impaired autophagy, aged AMPK-MKO mice possess a significant myopathy characterized by reduced muscle function, mitochondrial disease, and accumulation of the autophagy/mitophagy proteins p62 and Parkin.
Mitochondrial Dysfunction in Parkinson's Disease.
Review
New
Paek et al., Seoul, South Korea. In Exp Neurobiol, 30 Jun 2015
For the first time, we established human telomerase reverse transcriptase (hTERT)-immortalized wild type, idiopathic and Parkin deficient mesenchymal stromal cells (MSCs) isolated from the adipose tissues of PD patients, which could be used as a good cellular model to evaluate mitochondrial dysfunction for the better understanding of PD pathology and for the development of early diagnostic markers and effective therapy targets of PD.
How Mitochondrial Dynamism Orchestrates Mitophagy.
Review
New
Dorn et al., Beersheba, Israel. In Circ Res, 22 Jun 2015
Here, we review accumulating evidence supporting important roles for mitochondrial fission and fusion in cardiac mitochondrial quality control, focusing on the PTEN-induced putative kinase 1-Parkin mitophagy pathway.
Quantifying Ubiquitin Signaling.
Review
New
Harper et al., Boston, United States. In Mol Cell, 21 Jun 2015
Here, we review how quantitative proteomic tools and enrichment strategies are being used to quantify UB-dependent signaling systems, and to integrate UB signaling with regulatory phosphorylation events, illustrated with the PINK1/PARKIN pathway.
The three 'P's of mitophagy: PARKIN, PINK1, and post-translational modifications.
Review
New
Fon et al., Montréal, Canada. In Genes Dev, 15 Jun 2015
UNASSIGNED: Two Parkinson's disease (PD)-associated proteins, the mitochondrial kinase PINK1 and the E3-ubiquitin (Ub) ligase PARKIN, are central to mitochondrial quality control.
Phosphatase and tensin homolog-induced putative kinase 1 and Parkin in diabetic heart: Role of mitophagy.
Review
New
Long et al., Xi'an, China. In J Diabetes Investig, May 2015
Phosphatase and tensin homolog-induced putative kinase 1 (PINK1) and Parkin, initially identified to be associated with the pathogenesis of a familiar form of Parkinson's disease, have recently been recognized to play a critical role in mediating cardiomyocytes' adaption to stresses.
PINK1 and Parkin control localized translation of respiratory chain component mRNAs on mitochondria outer membrane.
New
Impact
Lu et al., Stanford, United States. In Cell Metab, Feb 2015
Here we show that Parkinson's disease (PD)-associated genes PINK1 and Parkin direct localized translation of certain nuclear-encoded RCC (nRCC) mRNAs.
The diabetes susceptibility gene Clec16a regulates mitophagy.
New
Impact
Stoffers et al., Philadelphia, United States. In Cell, Jul 2014
Here we report that Clec16a is a membrane-associated endosomal protein that interacts with E3 ubiquitin ligase Nrdp1.
The mitochondrial deubiquitinase USP30 opposes parkin-mediated mitophagy.
New
Impact
Sheng et al., San Francisco, United States. In Nature, Jul 2014
Here we report that USP30, a deubiquitinase localized to mitochondria, antagonizes mitophagy driven by the ubiquitin ligase parkin (also known as PARK2) and protein kinase PINK1, which are encoded by two genes associated with Parkinson's disease.
PARK2 orchestrates cyclins to avoid cancer.
New
Impact
Hodny et al., Praha, Czech Republic. In Nat Genet, Jun 2014
A new study identifies the PARK2 E3 ubiquitin ligase as an important coordinator of G1/S-phase cyclin turnover and explains how mutations targeting this key cell cycle regulatory node contribute to a range of cancers.
Meta-analysis of the influence of Parkin p.Asp394Asn variant on the susceptibility of Parkinson's disease.
GeneRIF
Sun et al., Beijing, China. In Neurosci Lett, 2012
This study does not support an association between the Parkin p.Asp394Asn variant and Parkinson disease risk.
PARK2 gene mutations in early onset Parkinson's disease patients of South India.
GeneRIF
Ramesh et al., Chennai, India. In Neurosci Lett, 2012
mutations in PARK2 gene may be a common cause of Parkinson's disease among South Indian early onset patients.
High frequency of Parkin exon rearrangements in Mexican-mestizo patients with early-onset Parkinson's disease.
GeneRIF
López López et al., Chiconcuac, Mexico. In Mov Disord, 2012
Patients with parkin exons 9 and 12 rearrangements showed a later age at onset than did cases with other regions affected, suggesting a mutational hot spot in the etiology of Mexican-mestizo patients with early-onset Parkinson's disease
Analysis of neural subtypes reveals selective mitochondrial dysfunction in dopaminergic neurons from parkin mutants.
GeneRIF
Pallanck et al., Seattle, United States. In Proc Natl Acad Sci U S A, 2012
study validates key tenets of the model that PINK1 and Parkin promote the fragmentation and turnover of depolarized mitochondria in dopaminergic neurons
Lewy body pathology and typical Parkinson disease in a patient with a heterozygous (R275W) mutation in the Parkin gene (PARK2).
GeneRIF
Giaccone et al., Milano, Italy. In Acta Neuropathol, 2012
report a patient with a heterozygous Parkin mutation (R275W, on exon 7), clinical features of typical Parkinson's disease and a neuropathological picture of diffuse Lewy body disease
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