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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 27 May 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
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.
Cytosolic PTEN-INDUCED PUTATIVE KINASE 1 is Stabilized By NF-κB Pathway and Promotes Non-Selective Mitophagy.
New
Lim et al., Singapore, Singapore. In J Biol Chem, 18 Jun 2015
UNASSIGNED: The potential cellular function of the 53 kDa cytosolic form of PINK1 (PINK1-53) is often overlooked due to its rapid degradation by the proteasome upon its production.
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.
Defining roles of PARKIN and ubiquitin phosphorylation by PINK1 in mitochondrial quality control using a ubiquitin replacement strategy.
New
Harper et al., Boston, United States. In Proc Natl Acad Sci U S A, 12 Jun 2015
UNASSIGNED: The PTEN-induced putative kinase protein 1 (PINK1) and ubiquitin (UB) ligase PARKIN direct damaged mitochondria for mitophagy.
Improvement Characteristics of Bio-active Materials Coated Fabric on Rat Muscular Mitochondria.
New
Ko et al., Seoul, South Korea. In Korean J Physiol Pharmacol, 31 May 2015
PINK1 expression did not change considerably and was inclined to decrease in control group, but the expression was down-regulated then subsequently increased with the use of the BMCF in a dose-dependent manner.
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.
Deubiquitinating enzymes regulate PARK2-mediated mitophagy.
New
McQuibban et al., Toronto, Canada. In Autophagy, 03 May 2015
The best-studied mitophagy pathway is the one mediated by PINK1 and PARK2/Parkin.
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.
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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