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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 15 Apr 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
Convergence of parkin, PINK1 and α-synuclein on stress-induced mitochondrial morphological remodelling.
New
Yao et al., United States. In J Biol Chem, 10 May 2015
UNASSIGNED: Mutations in parkin (PARK2), an ubiquitin ligase, cause early onset Parkinson's disease.
Linkıng a compound-heterozygous parkın mutant (Q311R and A371T) TO parkinson's dısease by usıng proteomıc and molecular approaches.
New
Iseri et al., Kocaeli, Turkey. In Neurochem Int, 09 May 2015
UNASSIGNED: Parkin is an E3-protein ubiquitin ligase, which plays an important role as a scavenger in cell metabolism.
iPS models of Parkin and PINK1.
New
Klein et al., Lübeck, Germany. In Biochem Soc Trans, 01 May 2015
Recessively inherited Parkin and PTEN-induced putative kinase 1 (PINK1) mutations have been investigated in this context and the present review describes the first insights gained from studies in iPSC-derived dopaminergic neurons, which comprise abnormalities in mitochondrial and dopamine homoeostasis, microtubular stability and axonal outgrowth.
The endoplasmic reticulum/mitochondria interface: a subcellular platform for the orchestration of the functions of the PINK1-Parkin pathway?
New
Corti et al., Paris, France. In Biochem Soc Trans, 01 May 2015
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.
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.
Molecular mechanisms underlying PINK1 and Parkin catalyzed ubiquitylation of substrates on damaged mitochondria.
Review
New
Matsuda et al., Tokyo, Japan. In Biochim Biophys Acta, 17 Mar 2015
UNASSIGNED: PINK1 and Parkin are gene products that cause genetic recessive Parkinsonism.
PINK1/Parkin-mediated mitophagy in mammalian cells.
Review
New
Okamoto et al., Suita, Japan. In Curr Opin Cell Biol, 16 Mar 2015
In mammalian cells, the Ser/Thr kinase PINK1 and the E3 ubiquitin ligase Parkin act cooperatively in sensing mitochondrial functional state and marking damaged mitochondria for disposal via the autophagy pathway.
Autophagy machinery in the context of mammalian mitophagy.
Review
New
Mizushima et al., Tokyo, Japan. In Biochim Biophys Acta, Feb 2015
PINK1-Parkin-dependent mitophagy has been extensively studied in the mammalian system.
The roles of PINK1, parkin, and mitochondrial fidelity in Parkinson's disease.
Review
New
Youle et al., Bethesda, United States. In Neuron, Feb 2015
PINK1 accumulates on the outer membrane of damaged mitochondria, activates Parkin's E3 ubiquitin ligase activity, and recruits Parkin to the dysfunctional mitochondrion.
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.
[CK2beta promotes Pink1/Parkin-mediated MIRO1 degradation].
New
Jiang et al., In Sheng Wu Yi Xue Gong Cheng Xue Za Zhi, Dec 2014
Studies have suggested that PINK1FL can selectively accumulate at the surface of damaged mitochondria and cooperate with another Parkinson's Disease-related protein PARKIN to trigger the degradation of MIRO1, a mitochondria trafficking regulator.
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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