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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 27 May 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
Parkin-induced ubiquitination of Mff promotes its association with p62/SQSTM1 during mitochondrial depolarization.
New
Jiang et al., Shenzhen, China. In Acta Biochim Biophys Sin (shanghai), 24 Jun 2015
UNASSIGNED: The ubiquitin ligase Parkin and autophagic adapter protein p62 are known to function in a common pathway controlling mitochondrial autophagy (mitophagy).
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.
A Versatile Strategy for the Semisynthetic Production of Ser65 Phosphorylated Ubiquitin and its Biochemical and Structural Characterization.
New
Virdee et al., Dundee, United Kingdom. In Chembiochem, 22 Jun 2015
This is exemplified by the phosphorylation of ubiquitin on Serine 65 by the Parkinson's disease-associated kinase PINK1 that mediates the activation of the E3 ligase Parkin.
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.
Parkin-mediated responses against infection and wound involve TSPO-VDAC complex in Drosophila.
New
Lee et al., Taegu, South Korea. In Biochem Biophys Res Commun, 13 Jun 2015
UNASSIGNED: Parkin, an E3 ubuquitin ligase associated with Parkinson's disease (PD), has recently been implicated in mediating innate immunity.
TBK1 controls autophagosomal engulfment of polyubiquitinated mitochondria through p62/SQSTM1 phosphorylation.
New
Nukina et al., Wako, Japan. In Hum Mol Genet, 13 Jun 2015
Here, we show that p62 phosphorylation at S403 is required for the efficient autophagosomal engulfment of polyubiquitinated mitochondria during Parkin-dependent mitophagy.
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, 31 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.
Selective removal of mitochondria via mitophagy: distinct pathways for different mitochondrial stresses.
Review
New
Chen et al., Beijing, China. In Biochim Biophys Acta, 01 May 2015
In mammals, different mitophagy effectors, including the mitophagy receptors NIX, BNIP3 and FUDNC1 and the PINK1/Parkin pathway, have been identified to participate in the selective clearance of mitochondria.
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.
Hepatitis B Virus X Protein Sensitizes TRAIL-Induced Hepatocyte Apoptosis by Inhibiting the E3 Ubiquitin Ligase A20.
New
Shi et al., Hangzhou, China. In Plos One, Dec 2014
Hepatitis B virus (HBV) infection causes hepatocyte death and liver damage, which may eventually lead to cirrhosis and liver cancer.
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.
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.
Pan-cancer genetic analysis identifies PARK2 as a master regulator of G1/S cyclins.
New
Impact
Chan et al., New York City, United States. In Nat Genet, Jun 2014
The PARK2 E3 ubiquitin ligase coordinately controls the stability of both cyclin D and cyclin E. Analysis of approximately 5,000 tumor genomes shows that PARK2 is a very frequently deleted gene in human cancer and uncovers a striking pattern of mutual exclusivity between PARK2 deletion and amplification of CCND1, CCNE1 or CDK4-implicating these genes in a common pathway.
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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