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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 30 Mar 2015.

PTEN induced putative kinase 1

PINK1, PARK6, PTEN-induced putative kinase 1
This gene encodes a serine/threonine protein kinase that localizes to mitochondria. It is thought to protect cells from stress-induced mitochondrial dysfunction. Mutations in this gene cause one form of autosomal recessive early-onset Parkinson disease. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: E3 ubiquitin ligase, PTEN, DJ-1, LRRK2, CAN
Papers using PINK1 antibodies
PINK1-dependent recruitment of Parkin to mitochondria in mitophagy
Supplier
Xia Xu-Gang et al., In International Journal of Biological Sciences, 2009
... PINK1 RNAi transgenic mice have been characterized ...
Mitochondrial rhomboid PARL regulates cytochrome c release during apoptosis via OPA1-dependent cristae remodeling.
Supplier
Green Douglas R., In PLoS Biology, 2005
... YFP-Parkin, YFP-Parkin mutants, mCherry-Parkin, PINK1-YFP, PINK1KD-YFP, PINK1 Δ1-110-YFP, and Opa3-PINK1 Δ1-110-YFP are in C1 or N1 Clontech vectors ...
Papers on PINK1
Roles of PTEN-induced putative kinase 1 and dynamin-related protein 1 in transient global ischemia-induced hippocampal neuronal injury.
New
Chuang et al., Kao-hsiung, Taiwan. In Biochem Biophys Res Commun, 17 Apr 2015
UNASSIGNED: Recent studies showed that increased mitochondrial fission is an early event of cell death during cerebral ischemia and dynamin-related protein 1 (Drp1) plays an important role in mitochondrial fission, which may be regulated by PTEN-induced putative kinase 1 (PINK1), a mitochondrial serine/threonine-protein kinase thought to protect cells from stress-induced mitochondrial dysfunction and regulate mitochondrial fission.
Evidence for a common biological pathway linking three Parkinson's disease-causing genes: parkin, PINK1 and DJ-1.
New
Bardien et al., Cape Town, South Africa. In Eur J Neurosci, 11 Apr 2015
Autosomal recessive, early-onset cases of PD are predominantly caused by mutations in the parkin, PINK1 and DJ-1 genes.
Mitochondrial dysfunction and mitophagy in Parkinson's: from familial to sporadic disease.
Review
New
Wade-Martins et al., Montréal, Canada. In Trends Biochem Sci, 07 Apr 2015
Recently, the mechanisms by which PD-associated mitochondrial proteins phosphatase and tensin homolog deleted on chromosome 10 (PTEN)-induced putative kinase 1 (PINK1) and parkin function and induce neurodegeneration have been identified.
Mask loss-of-function rescues mitochondrial impairment and muscle degeneration of Drosophila pink1 and parkin mutants.
New
Wu et al., New Orleans, United States. In Hum Mol Genet, 05 Apr 2015
UNASSIGNED: PTEN-induced kinase 1 (Pink1) and ubiquitin E3 ligase Parkin function in a linear pathway to maintain healthy mitochondria via regulating mitochondrial clearance and trafficking.
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, 26 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, 21 Feb 2015
Biochemical and genetic studies reveal that the products of two genes that are mutated in autosomal recessive parkinsonism, PINK1 and Parkin, normally work together in the same pathway to govern mitochondrial quality control, bolstering previous evidence that mitochondrial damage is involved in Parkinson's disease.
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, 06 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.
Epithelial Cell Mitochondrial Dysfunction and PINK1 Are Induced by Transforming Growth Factor- Beta1 in Pulmonary Fibrosis.
New
Morse et al., Boston, United States. In Plos One, Dec 2014
METHODS: We studied markers of mitochondrial injury and the mitophagy marker, PTEN-induced putative kinase 1 (PINK1), in IPF lung tissues by Western blotting, transmission electron microscopy (TEM), and immunofluorescence.
The Broad Impact of TOM40 on Neurodegenerative Diseases in Aging.
New
Chiba-Falek et al., Durham, United States. In J Parkinsons Dis Alzheimers Dis, Nov 2014
Healthy mitochondria normally import and degrade the PD-related protein Pink1, but Pink1 exits mitochondria if the membrane potential collapses and initiates Parkin-mediated mitophagy.
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.
Ubiquitin is phosphorylated by PINK1 to activate parkin.
New
Impact
Matsuda et al., Tokyo, Japan. In Nature, Jul 2014
PINK1 (PTEN induced putative kinase 1) and PARKIN (also known as PARK2) have been identified as the causal genes responsible for hereditary recessive early-onset Parkinsonism.
Defective mitophagy in XPA via PARP-1 hyperactivation and NAD(+)/SIRT1 reduction.
New
Impact
Bohr et al., Baltimore, United States. In Cell, Jun 2014
XPA-deficient cells show defective mitophagy with excessive cleavage of PINK1 and increased mitochondrial membrane potential.
PTENα, a PTEN isoform translated through alternative initiation, regulates mitochondrial function and energy metabolism.
New
Impact
Yin et al., Beijing, China. In Cell Metab, Jun 2014
PTENα interacts with canonical PTEN to increase PINK1 protein levels and promote energy production.
Inactivation of Pink1 gene in vivo sensitizes dopamine-producing neurons to 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) and can be rescued by autosomal recessive Parkinson disease genes, Parkin or DJ-1.
GeneRIF
Park et al., Ottawa, Canada. In J Biol Chem, 2012
This evidence not only provides strong evidence for the role of endogenous Pink1 in neuronal survival, but also supports a role of DJ-1 and Parkin acting parallel or downstream of endogenous Pink1 to mediate survival in a mammalian in vivo context.
Pink1 kinase and its membrane potential (Deltaψ)-dependent cleavage product both localize to outer mitochondrial membrane by unique targeting mode.
GeneRIF
Voos et al., Bonn, Germany. In J Biol Chem, 2012
Multiple targeting signals featured by the Pink1 sequence result in the final localization of both the full-length protein and its major Deltapsi-dependent cleavage product to the cytosolic face of the outer mitochondrial membrane.
Vitamin K2 is a mitochondrial electron carrier that rescues pink1 deficiency.
Impact
GeneRIF
Verstreken et al., Leuven, Belgium. In Science, 2012
study identified UBIAD1/Heix as a modifier of pink1
Regulation of mitochondrial permeability transition pore by PINK1.
GeneRIF
Shen et al., Boston, United States. In Mol Neurodegener, 2011
Our findings show that loss of PINK1 causes selective increases in mitochondrial permeability transition pore opening and mitochondrial calcium
Expression of Pink1 with α-synuclein in the dopaminergic neurons of Drosophila leads to increases in both lifespan and healthspan.
GeneRIF
Staveley et al., St. John's, Canada. In Genet Mol Res, 2011
Increased expression of alpha-synuclein and Pink1 together have a synergistic effect, allowing for enhanced protection and increased survival of the organism.
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