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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 28 Nov 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
Early Expression of Parkinson's Disease-Related Mitochondrial Abnormalities in PINK1 Knockout Rats.
New
Fox et al., Omaha, United States. In Mol Neurobiol, 25 Dec 2014
UNLABELLED: PTEN-induced kinase 1 (PINK1) mutations are responsible for an autosomal recessive, familial form of Parkinson's disease.
The Complex I Subunit NDUFA10 Selectively Rescues Drosophila pink1 Mutants through a Mechanism Independent of Mitophagy.
New
Whitworth et al., Sheffield, United Kingdom. In Plos Genet, 30 Nov 2014
Mutations in PINK1, a mitochondrially targeted serine/threonine kinase, cause autosomal recessive Parkinson's disease (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.
Parkin and PINK1: much more than mitophagy.
Review
New
Dawson et al., Baltimore, United States. In Trends Neurosci, Jun 2014
In support of this theory, data from multiple PD models have linked Phosphatase and tensin homolog (PTEN)-induced putative kinase 1 (PINK1) and parkin, two recessive PD genes, in a common pathway impacting mitochondrial health, prompting a flurry of research to identify their mitochondrial targets.
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.
Elevated Autophagy and Mitochondrial Dysfunction in the Smith-Lemli-Opitz Syndrome.
New
Tulenko et al., Nashville, United States. In Mol Genet Metab Rep, Dec 2013
In addition, the levels of PINK1 which targets dysfunctional mitochondria for removal by the autophagic pathway are elevated in SLOS cells, consistent with mitochondrial dysfunction as a stimulant of mitophagy in SLOS.
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.
Emerging modes of PINK1 signaling: another task for MARK2.
Review
New
Mandelkow et al., Hamburg, Germany. In Front Mol Neurosci, Dec 2013
PTEN-induced kinase 1 (PINK1) acts at multiple levels to promote mitochondrial health, including regulatory influence on ATP-synthesis, protein quality control, apoptosis, mitochondrial transport, and destiny.
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.
Acute focal brain damage alters mitochondrial dynamics and autophagy in axotomized neurons.
New
D'Amelio et al., Roma, Italy. In Cell Death Dis, Dec 2013
We provided evidence that lesion of a cerebellar hemisphere causes mitochondria depolarization in axotomized precerebellar neurons associated with PTEN-induced putative kinase 1 accumulation and Parkin translocation to mitochondria, block of mitochondrial fusion by Mfn1 degradation, increase of calcineurin activity and dynamin-related protein 1 translocation to mitochondria, and consequent mitochondrial fission.
High-Content Functional Genomic Screening to Identify Novel Regulators of the PINK1-Parkin Pathway.
New
Screaton et al., Ottawa, Canada. In Methods Enzymol, Dec 2013
PINK1/PARK6 and Parkin/PARK2 are amongst the most commonly mutated genes associated with recessive forms of familial 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.
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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