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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 29 Mar 2014.

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, DJ-1, PTEN, 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
K27 ubiquitination of the mitochondrial transport protein Miro is dependent on serine 65 of the Parkin ubiquitin ligase.
New
Kittler et al., London, United Kingdom. In J Biol Chem, 26 Apr 2014
Here we demonstrate that Miro1, an outer mitochondrial membrane (OMM) protein crucial for the regulation of mitochondrial trafficking and distribution, is a substrate of the PINK1/Parkin mitochondrial quality control system in human dopaminergic neuroblastoma cells.
Parkin is activated by PINK1-dependent phosphorylation of ubiquitin at Serine65.
New
Muqit et al., In Biochem J, 25 Apr 2014
UNLABELLED: We have previously reported that the Parkinson's disease associated PINK1 kinase is activated by mitochondrial depolarisation and stimulates the Parkin E3 ligase by phosphorylating Serine65 (Ser65) within its ubiquitin like (Ubl) domain.
PINK1 Loss of Function Mutations Affect Mitochondrial Complex I Activity via NdufA10 Ubiquinone Uncoupling.
New
Impact
De Strooper et al., Leuven, Belgium. In Science, 20 Apr 2014
UNLABELLED: Under resting conditions, Pink1 knockout cells and cells derived from patients with PINK1 mutations display a loss of mitochondrial complex I reductive activity causing a decrease in the mitochondrial membrane potential.
Genetic mutations in early-onset Parkinson's disease Mexican patients: Molecular testing implications.
New
López-López et al., Chiconcuac, Mexico. In Am J Med Genet B Neuropsychiatr Genet, 23 Mar 2014
UNLABELLED: Mutations in PARK2, PINK1, and DJ-1 have been associated with autosomal recessive early-onset Parkinson's disease.
Enhancing nucleotide metabolism protects against mitochondrial dysfunction and neurodegeneration in a PINK1 model of Parkinson's disease.
New
Impact
Martins et al., Bonn, Germany. In Nat Cell Biol, 28 Feb 2014
Mutations in PINK1 cause early-onset Parkinson's disease (PD).
High-content genome-wide RNAi screens identify regulators of parkin upstream of mitophagy.
New
Impact
Youle et al., Bethesda, United States. In Nature, Jan 2014
Recent studies of the Parkinson's disease associated genes PINK1 (ref.
The impact of reactive oxygen species and genetic mitochondrial mutations in Parkinson's disease.
Review
New
Motherwell et al., United States. In Gene, Jan 2014
The genetic mutations of Parkinson's related proteins such as PINK1 and LRRK2 contribute to mitochondrial dysfunction which precedes ROS formation.
Mismatch repair deficiency in ovarian cancer - Molecular characteristics and clinical implications.
Review
New
Gourley et al., Edinburgh, United Kingdom. In Gynecol Oncol, Jan 2014
Investigation of MMR related synthetic lethality in colorectal cancer has identified dihydrofolate reductase, DNA polymerase β and DNA polymerase γ and PTEN-induced putative kinase 1 as synthetic lethal to certain MMR defects by causing accumulation of oxidative DNA damage.
Phosphorylation of Parkin at Serine65 is essential for activation: elaboration of a Miro1 substrate-based assay of Parkin E3 ligase activity.
New
Muqit et al., Dundee, United Kingdom. In Open Biol, Dec 2013
Mutations in PINK1 and Parkin are associated with early-onset Parkinson's disease.
Antiaging Properties of a Grape-Derived Antioxidant Are Regulated by Mitochondrial Balance of Fusion and Fission Leading to Mitophagy Triggered by a Signaling Network of Sirt1-Sirt3-Foxo3-PINK1-PARKIN.
New
Das et al., Farmington, United States. In Oxid Med Cell Longev, Dec 2013
The present study on ischemic reperfusion (I/R) in rat hearts demonstrates that Foxo3a is activated subsequent to Sirt3 activation, which then activates PINK1.
Mitochondrial quality control in neurodegenerative diseases.
Review
New
Dupuis, Strasbourg, France. In Biochimie, Sep 2013
UNLABELLED: Mutations causing genetic forms of Parkinson's disease or hereditary neuropathies have been recently shown to affect key molecular players involved in the recycling of defective mitochondria, most notably PARKIN, PINK1, Mitofusin 2 or dynein heavy chain.
Bumping up kinase activity with an ATP-derived neo-substrate.
New
Impact
Kapoor et al., New York City, United States. In Cell, Sep 2013
In this issue, Hertz et al. report an innovative approach for activating the Parkinson's-associated kinase PINK1 in cells with an ATP-derived neo-substrate.
A neo-substrate that amplifies catalytic activity of parkinson's-disease-related kinase PINK1.
New
Impact
Shokat et al., San Francisco, United States. In Cell, Sep 2013
Mutations in the mitochondrial kinase PINK1 that reduce kinase activity are associated with mitochondrial defects and result in an autosomal-recessive form of early-onset PD.
Lysosomal impairment in Parkinson's disease.
Review
New
Bezard et al., Bordeaux, France. In Mov Disord, Jun 2013
Furthermore, other PD-related genes, such as leucine-rich repeat kinase-2 (LRRK2), parkin, and phosphatase and tensin homolog (PTEN)-induced putative kinase 1 (PINK1), have been mechanistically linked to alterations in ALPs.
Diversity of mitochondrial pathology in a mouse model of axonal degeneration in synucleinopathies.
Review
Hashimoto et al., Tokyo, Japan. In Oxid Med Cell Longev, 2012
In particular, recent studies have demonstrated that failure of mitochondrial quality control caused by loss of function of the PTEN-induced kinase 1 (PINK1, PARK6) Parkin (PARK2) pathway may be causative in some familial PD.
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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