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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

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, CAN, Ubiquitin
Papers using PINK1 antibodies
PINK1-dependent recruitment of Parkin to mitochondria in mitophagy
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.
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
PARK2 enhancement is able to compensate mitophagy alterations found in sporadic Alzheimer's disease.
García-Escudero et al., Madrid, Spain. In Hum Mol Genet, Jan 2016
Impairment in mitophagy has been proven in these cells due to diminished PARK2 and insufficient vesicle induction, accumulating depolarized mitochondria and PINK1.
PGC-1α Overexpression via Local Transfection Attenuates Mitophagy Pathway in Muscle Disuse Atrophy.
Ji et al., Minneapolis, United States. In Free Radic Biol Med, Jan 2016
While mitochondrial biogenesis and antioxidant enzymes are decreased, all autophagic and mitophagic protein markers such as Beclin-1, Bnip3, PINK1, parkin, Mul 1 and the LC3II/LC3I ratio were increased in IM-RM muscle together with activation of FoxO pathway.
Dopamine induces mitochondrial depolarization without activating PINK1-mediated mitophagy.
Alberio et al., Busto Arsizio, Italy. In J Neurochem, Jan 2016
Indeed, PINK1 did not accumulate on the outer mitochondrial membrane, nor was parkin recruited to depolarized mitochondria.
Parkin-mediated mitophagy directs perinatal cardiac metabolic maturation in mice.
Dorn et al., Saint Louis, United States. In Science, Jan 2016
Here, we found that PINK1-Mfn2-Parkin-mediated mitophagy directs this metabolic transformation in mouse hearts.
Parkinson's disease proteins: Novel mitochondrial targets for cardioprotection.
Hausenloy et al., Singapore, Singapore. In Pharmacol Ther, Dec 2015
In dopaminergic neurons of the substantia nigra, these PD proteins, which include Parkin, PINK1, DJ-1, LRRK2, and α-synuclein, play essential roles in preventing cell death-through maintaining normal mitochondrial function, protecting against oxidative stress, mediating mitophagy, and preventing apoptosis.
Ubiquitin phosphorylation in Parkinson's disease: Implications for pathogenesis and treatment.
Li et al., Atlanta, United States. In Transl Neurodegener, Dec 2015
The identification of mutations in mitochondrial serine/threonine kinase PINK1 or E3 ubiquitin-protein ligase parkin as the cause of autosomal recessive PD opens up new avenues for uncovering neuroprotective pathways and PD pathogenic mechanisms.
In Vitro Comparison of the Activity Requirements and Substrate Specificity of Human and Triboleum castaneum PINK1 Orthologues.
Morais et al., Leuven, Belgium. In Plos One, Dec 2015
Mutations in the gene encoding the mitochondrial kinase PINK1 cause early-onset familial Parkinson's disease.
PINK1 expression increases during brain development and stem cell differentiation, and affects the development of GFAP-positive astrocytes.
Joe et al., Suwŏn, South Korea. In Mol Brain, Dec 2015
BACKGROUND: Mutation of PTEN-induced putative kinase 1 (PINK1) causes autosomal recessive early-onset Parkinson's disease (PD).
Parkin-dependent mitophagy in the heart.
Dorn, Saint Louis, United States. In J Mol Cell Cardiol, Dec 2015
Here, the evidence supporting a role for the prototypical mitochondrial quality control pathway, PINK1-Parkin mediated mitophagy, in cardiac homeostasis and heart disease is reviewed.
Counteracting PINK/Parkin deficiency in the activation of mitophagy: a potential therapeutic intervention for Parkinson's Disease.
Ziviani et al., Padova, Italy. In Curr Neuropharmacol, Nov 2015
UNASSIGNED: Parkinson's Disease (PD) related genes PINK1, a protein kinase1, and Parkin, an E3 ubiquitin ligase2,operate within the same pathway3-5, which controls, via specific elimination of dysfunctional mitochondria, the quality of the organelle network6.
Mechanism of phospho-ubiquitin-induced PARKIN activation.
Komander et al., Cambridge, United Kingdom. In Nature, Sep 2015
The E3 ubiquitin ligase PARKIN (encoded by PARK2) and the protein kinase PINK1 (encoded by PARK6) are mutated in autosomal-recessive juvenile Parkinsonism (AR-JP) and work together in the disposal of damaged mitochondria by mitophagy.
The ubiquitin kinase PINK1 recruits autophagy receptors to induce mitophagy.
Youle et al., Bethesda, United States. In Nature, Sep 2015
To initiate mitophagy, the ubiquitin kinase PINK1 phosphorylates ubiquitin to activate the ubiquitin ligase parkin, which builds ubiquitin chains on mitochondrial outer membrane proteins, where they act to recruit autophagy receptors.
PINK1 and Parkin control localized translation of respiratory chain component mRNAs on mitochondria outer membrane.
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.
MIRO GTPases in Mitochondrial Transport, Homeostasis and Pathology.
Tang, Singapore, Singapore. In Cells, 2014
Recent findings have revealed a myriad of molecules that are associated with MIRO, particularly the kinesin adaptor Milton/TRAK, mitofusin, PINK1 and Parkin, as well as the endoplasmic reticulum-mitochondria encounter structure (ERMES) complex.
The mitochondrial deubiquitinase USP30 opposes parkin-mediated mitophagy.
Sheng et al., San Francisco, United States. In Nature, 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.
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.
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.
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.
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.
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.
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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