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

Presenilin associated, rhomboid-like

PARL, Pbeta
This gene encodes a mitochondrial integral membrane protein. Following proteolytic processing of this protein, a small peptide (P-beta) is formed and translocated to the nucleus. This gene may be involved in signal transduction via regulated intramembrane proteolysis of membrane-tethered precursor proteins. Variation in this gene has been associated with increased risk for type 2 diabetes. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Jul 2008] (from NCBI)
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Top mentioned proteins: CAN, ACID, Presenilin-1, HAD, lacZ
Papers on PARL
Mutation analyses and association studies to assess the role of the presenilin-associated rhomboid-like gene in Parkinson's disease.
Krüger et al., Tübingen, Germany. In Neurobiol Aging, Jan 2016
UNASSIGNED: Presenilin-associated rhomboid-like (PARL), a serine protease located in the inner mitochondrial membrane, has been shown to genetically interact and process PTEN-induced putative kinase a protein known for its critical role in mitochondrial homeostasis and early-onset forms of Parkinson's disease (PD).
Common variants of the PINK1 and PARL genes do not confer genetic susceptibility to schizophrenia in Han Chinese.
Yao et al., Kunming, China. In Mol Genet Genomics, Apr 2015
Phosphatase and tension homologue-induced kinase 1 (PINK1) and presenilin-associated rhomboid-like protease (PARL) are mitochondrial proteins, and genetic variants of these two genes may confer genetic susceptibility to schizophrenia by influencing mitochondrial function.
Differential evolution of members of the rhomboid gene family with conservative and divergent patterns.
Ma et al., Shanghai, China. In New Phytol, Apr 2015
Our results showed that eukaryotic rhomboids could be divided into five subfamilies (RhoA-RhoD and PARL).
Intramembrane protease PARL defines a negative regulator of PINK1- and PARK2/Parkin-dependent mitophagy.
Lemberg et al., Heidelberg, Germany. In Autophagy, 2014
Here we show that ablation of the mitochondrial rhomboid protease PARL leads to retrograde translocation of an intermembrane space-bridging PINK1 import intermediate.
A Mitofusin-2-dependent inactivating cleavage of Opa1 links changes in mitochondria cristae and ER contacts in the postprandial liver.
Pellegrini et al., Québec, Canada. In Proc Natl Acad Sci U S A, 2014
This processing of Opa1, termed C-cleavage, is mediated by the activity of a cysteine protease whose activity is independent from that of Oma1 and presenilin-associated rhomboid-like (PARL), two known Opa1 regulators.
Identification of the variants in PARL, the nuclear modifier gene, responsible for the expression of LHON patients in Thailand.
Lertrit et al., Bangkok, Thailand. In Exp Eye Res, 2013
The present study explored variation in the PARL gene as one of the potential nuclear modifiers in the pathogenesis of Leber hereditary optic neuropathy (LHON).
Rhomboid proteins: a role in keratinocyte proliferation and cancer.
Blaydon et al., London, United Kingdom. In Cell Tissue Res, 2013
Rhomboids typically contain six or seven transmembrane domains (TMD) and have been classified into four subgroups: Secretase A and B, Presenilin-Associated-Rhomboid-Like (PARL) and iRhoms.
Rhomboid proteases in mitochondria and plastids: keeping organelles in shape.
Pellegrini et al., Québec, Canada. In Biochim Biophys Acta, 2013
Among eukaryotes, a distinct subfamily of rhomboids, prototyped by the mammalian mitochondrial protein Parl, ensures the maintenance of the structural and functional integrity of mitochondria and plastids.
The p.S77N presenilin-associated rhomboid-like protein mutation is not a frequent cause of early-onset Parkinson's disease.
Djarmati et al., In Mov Disord, 2011
p.S77N variant, and, possibly, mutations in the PARL protein overall, are not a frequent cause of autosomal recessive early-onset Parkinson's disease
Structural and mechanistic basis of Parl activity and regulation.
Pellegrini et al., Québec, Canada. In Cell Death Differ, 2011
work provides unexpected insights into the structural determinants regulating Parl stability and activity in vivo, and reveals a complex cascade of proteolytic events controlling the function of the protease in the mitochondrion
The mitochondrial intramembrane protease PARL cleaves human Pink1 to regulate Pink1 trafficking.
Lemberg et al., Heidelberg, Germany. In J Neurochem, 2011
the PARL-catalyzed removal of the Pink1 signal sequence in the canonical import pathway acts as a cellular checkpoint for mitochondrial integrity
Functional alteration of PARL contributes to mitochondrial dysregulation in Parkinson's disease.
Bulman et al., Toronto, Canada. In Hum Mol Genet, 2011
PARL deficiency impairs PARKIN recruitment to mitochondria.
PINK1 cleavage at position A103 by the mitochondrial protease PARL.
Wood et al., London, United Kingdom. In Hum Mol Genet, 2011
Mitochondrial protease PARL cleaves PINK1 at position A103.
The PARL family of mitochondrial rhomboid proteases.
Pellegrini et al., Baltimore, United States. In Semin Cell Dev Biol, 2010
This "1+6" structure, which is shared only among mitochondrial rhomboids, defines a subfamily of rhomboids with the prototypical family member being mammalian Parl.
Regulation of skeletal muscle oxidative capacity and insulin signaling by the mitochondrial rhomboid protease PARL.
Ravussin et al., Baton Rouge, United States. In Cell Metab, 2010
Suppression of PARL protein in healthy myotubes lowered mitochondrial mass and insulin-stimulated glycogen synthesis and increased reactive oxygen species production.
Emerging roles of mitochondrial proteases in neurodegeneration.
Rugarli et al., Milano, Italy. In Biochim Biophys Acta, 2010
The mitochondrial proteases HTRA2 and PARL increase the susceptibility of neurons to apoptotic cell death.
Hax1-mediated processing of HtrA2 by Parl allows survival of lymphocytes and neurons.
Ihle et al., Memphis, United States. In Nature, 2008
Hax1, is required to suppress apoptosis in lymphocytes and neurons; suppression requires the interaction of Hax1 with the mitochondrial proteases Parl and HtrA2
Mitochondrial rhomboid PARL regulates cytochrome c release during apoptosis via OPA1-dependent cristae remodeling.
De Strooper et al., Padova, Italy. In Cell, 2006
Parl-/- mitochondria display reduced levels of OPA1, and OPA1 specifically targeted to IMS complements Parl-/- cells, substantiating the importance of PARL in OPA1 processing.(PARL protein, mouse)
OPA1 and PARL keep a lid on apoptosis.
Gottlieb, Glasgow, United Kingdom. In Cell, 2006
In this issue of Cell, Cipolat et al. and Frezza et al. (2006) show that a rhomboid intramembrane protease PARL and a dynamin-related protein OPA1 are critical regulators of cristae remodeling.
Mitochondrial membrane remodelling regulated by a conserved rhomboid protease.
Freeman et al., Cambridge, United Kingdom. In Nature, 2003
In addition, mitochondrial rhomboids are conserved throughout eukaryotes and the mammalian homologue, PARL, rescues the yeast mutant, suggesting that these proteins represent a functionally conserved subclass of rhomboid proteases.
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