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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 10 Dec 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, 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
Motor phenotype of LRRK2-associated Parkinson's disease: A tunisian longitudinal study.
New
Hentati et al., Tunisia. In Mov Disord, 09 Jan 2015
Fifty-eight patients diagnosed with PD-related LRRK2 G2019S mutation were included in the study and compared with 54 sporadic PD patients with negative tests for LRRK2 G2019S, PINK1, SNCA, PRKN, and DJ1 mutations.
TSPO interacts with VDAC1 and triggers a ROS-mediated inhibition of mitochondrial quality control.
New
Campanella et al., London, United Kingdom. In Autophagy, 03 Jan 2015
Here, we report that TSPO inhibits mitochondrial autophagy downstream of the PINK1-PARK2 pathway, preventing essential ubiquitination of proteins.
Glutamate excitotoxicity in neurons triggers mitochondrial and endoplasmic reticulum accumulation of Parkin, and, in the presence of N-acetyl cysteine, mitophagy.
New
Berman et al., Pittsburgh, United States. In Neurobiol Dis, 02 Jan 2015
Models using mitochondrial stressors in numerous cell types have elucidated a PINK1-dependent pathway whereby Parkin accumulates on damaged mitochondria and targets them for mitophagy.
Phosphorylation of Mitochondrial Polyubiquitin by PINK1 Promotes Parkin Mitochondrial Tethering.
New
Imai et al., Tokyo, Japan. In Plos Genet, 31 Dec 2014
The kinase PINK1 and the E3 ubiquitin (Ub) ligase Parkin participate in mitochondrial quality control.
ROS act as an upstream signal to mediate cadmium-induced mitophagy in mouse brain.
New
Zhang et al., Lanzhou, China. In Neurotoxicology, 22 Dec 2014
Meanwhile, Cd induced mitophagy, as indicated by the collapse of mitochondrial membrane potential (MMP), formation of mitophagosomes, increases of PINK1 level and LC3-II/LC3-I ratio and decrease of mitochondrial mass.
PINK1 signaling in cancer biology.
Review
New
O'Neill et al., Cork, Ireland. In Biochim Biophys Acta, 23 Nov 2014
UNLABELLED: PTEN-induced kinase 1 (PINK1) was identified initially in cancer cells as a gene up-regulated by overexpression of the major tumor suppressor, PTEN.
Inflammation is genetically implicated in Parkinson's disease.
Review
New
Halliday et al., Sydney, Australia. In Neuroscience, 22 Nov 2014
Relatively rare missense mutations in genes such as LRRK2, Parkin, SNCA and PINK1 are causative for familial PD whereas more common variation in genes, including LRRK2, SNCA and GBA, comprise risk factors for sporadic PD.
A new pathway for mitochondrial quality control: mitochondrial-derived vesicles.
Review
New
McBride et al., Montréal, Canada. In Embo J, Sep 2014
The Parkinson's disease-associated proteins Vps35, Parkin, and PINK1 are involved in the biogenesis of a subset of these MDVs, linking this novel trafficking pathway to human disease.
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.
PINK1 loss-of-function mutations affect mitochondrial complex I activity via NdufA10 ubiquinone uncoupling.
New
Impact
De Strooper et al., Leuven, Belgium. In Science, May 2014
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.
The degeneration and replacement of dopamine cells in Parkinson's disease: the role of aging.
Review
New
Sabate et al., Santa Cruz de Tenerife, Spain. In Front Neuroanat, Dec 2013
Proteins involved in PD such as α-synuclein, UCH-L1, PINK1 or DJ-1, are also involved in aging.
Parkinson's disease-implicated kinases in the brain; insights into disease pathogenesis.
Review
New
Halliday et al., Australia. In Front Mol Neurosci, Dec 2013
Elevated phosphorylation of the PD-defining pathological protein, α-synuclein, correlates with its aggregation and toxic accumulation in neurons, whilst genetic missense mutations in the kinases PTEN-induced putative kinase 1 and leucine-rich repeat kinase 2, increase susceptibility to PD. Experimental evidence also links kinases of the phosphoinositide 3-kinase and mitogen-activated protein kinase signaling pathways, amongst others, to PD. Understanding how the levels or activities of these enzymes or their substrates change in brain tissue in relation to pathological states can provide insight into disease pathogenesis.
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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