ArticleBiochimica et biophysica acta2010
Evidence for proteolytic processing and stimulated organelle redistribution of iPLA(2)beta.
Article in Biochimica et biophysica acta, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 32 citations in OpenAlex.
- Phospholipases: Where Do We Stand?Methods in molecular biology (Clifton, N.J.) · 2027Review
- Parkinson's disease-associated PLA2G6 protects IP3R1 protein to control ER-mitochondria tethering and CaNature communications · 2026Article
- The balancing act between lipid droplets and lysosomes for membrane functionality in age-related neurodegeneration and inflammation.Progress in lipid research · 2025Review
- The PNPLA family of enzymes: characterisation and biological role.Arhiv za higijenu rada i toksikologiju · 2023Article
- Molecular basis of unique specificity and regulation of group VIA calcium-independent phospholipase APharmacology & therapeutics · 2023Review
- Alterations in β-Cell Sphingolipid Profile Associated with ER Stress and iPLAMolecules (Basel, Switzerland) · 2021Article
- iPLACells · 2021Article
- Antioxidant Synergy of Mitochondrial Phospholipase PNPLA8/iPLA2γ with Fatty Acid-Conducting SLC25 Gene Family Transporters.Antioxidants (Basel, Switzerland) · 2021Review
- The Impact of the CaBiomolecules · 2021Review
- Omega-3 versus Omega-6 fatty acid availability is controlled by hydrophobic site geometries of phospholipase AJournal of lipid research · 2021Article
- iPLA2-VIA is required for healthy aging of neurons, muscle, and the female germline in Drosophila melanogaster.PloS one · 2021Article
- Mitochondrial Dysfunction, Oxidative Stress and Neuroinflammation in Neurodegeneration with Brain Iron Accumulation (NBIA).Antioxidants (Basel, Switzerland) · 2020Review
- Rescue of Hepatic Phospholipid Remodeling Defectin iPLA2β-Null Mice Attenuates Obese but Not Non-Obese Fatty Liver.Biomolecules · 2020Review
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- Substrate-Specific Inhibition Constants for Phospholipase AJournal of medicinal chemistry · 2019Article
- Review: Insights into molecular mechanisms of disease in neurodegeneration with brain iron accumulation: unifying theories.Neuropathology and applied neurobiology · 2016Review
- Mitochondrial dysfunction and defects in lipid homeostasis as therapeutic targets in neurodegeneration with brain iron accumulation.Rare diseases (Austin, Tex.) · 2016Article
- Calcium-independent phospholipases A2 and their roles in biological processes and diseases.Journal of lipid research · 2015Review
- Group VIA phospholipase A2 mitigates palmitate-induced β-cell mitochondrial injury and apoptosis.The Journal of biological chemistry · 2014Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Over the past decade, important roles for the 84-88kDa Group VIA Ca(2+)-independent phospholipase A(2) (iPLA(2)beta) in various organs have been described. We demonstrated that iPLA(2)beta participates in insulin secretion, insulinoma cells and native pancreatic islets express full-length and truncated isoforms of iPLA(2)beta, and certain stimuli promote perinuclear localization of iPLA(2)beta. To gain a better understanding of its mobilization, iPLA(2)beta was expressed in INS-1 cells as a fusion protein with EGFP, enabling detection of subcellular localization of iPLA(2)beta by monitoring EGFP fluorescence. Cells stably-transfected with fusion protein expressed nearly 5-fold higher catalytic iPLA(2)beta activity than control cells transfected with EGFP cDNA alone, indicating that co-expression of EGFP does not interfere with manifestation of iPLA(2)beta activity. Dual fluorescence monitoring of EGFP and organelle Trackers combined with immunoblotting analyses revealed expression of truncated iPLA(2)beta isoforms in separate subcellular organelles. Exposure to secretagogues and induction of ER stress are known to activate iPLA(2)beta in beta-cells and we find here that these stimuli promote differential localization of iPLA(2)beta in subcellular organelles. Further, mass spectrometric analyses identified iPLA(2)beta variants from which N-terminal residues were removed. Collectively, these findings provide evidence for endogenous proteolytic processing of iPLA(2)beta and redistribution of iPLA(2)beta variants in subcellular compartments. It might be proposed that in vivo processing of iPLA(2)beta facilitates its participation in multiple biological processes.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.