Gene Ontology annotation through association of InterPro records with GO terms.
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Electronic Gene Ontology annotations created by transferring manual GO annotations between related proteins based on shared sequence features.
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara.
Combined Automated Annotation using Multiple IEA Methods.
Proteomic analysis of rat liver peroxisome - presence of peroxisome-specific isozyme of Lon protease.
Contribution of peroxisome-specific isoform of Lon protease in sorting PTS1 proteins to peroxisomes.
Defining the membrane proteome of NK cells.
Two proteases, trypsin domain-containing 1 (Tysnd1) and peroxisomal lon protease (PsLon), cooperatively regulate fatty acid β-oxidation in peroxisomal matrix.
An organelle-specific protein landscape identifies novel diseases and molecular mechanisms.
Architecture of the human interactome defines protein communities and disease networks.
A reference map of the human binary protein interactome.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
Cargo of PEX5S,L translocates from the cytosol to the peroxisomal matrix
PEX5S,L Cargo binds PEX13-PEX14-PEX2-PEX10-PEX12 (Docking and Translocation Module)
Deep research on LONP2 function
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Comprehensive review of LONP2 structure, function, and disease associations
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ATP-dependent serine protease in peroxisomal matrix
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Contains Lon N domain, AAA+ ATPase domain, and proteolytic domain with Ser-Lys dyad
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Functions in protein quality control, PTS2 protein processing, fatty acid beta-oxidation regulation
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Has ATP-independent chaperone activity
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Concentrated in peroxisomal crystalline core
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Mutations cause Buratti-Harel syndrome
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Upregulated in cervical cancer
Falcon deep research on LONP2 function (Edison Scientific Literature)
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LONP2 is the only known peroxisomal protease conserved in plants, fungi, and mammals; it arose as an early gene duplication from the mitochondrial paralog LONP1.
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Acute siRNA-mediated LONP2 depletion in COS-7 and U2OS cells causes accumulation of self-cleaved TYSND1, fewer but enlarged/elongated peroxisomes, and selective failure of CFP-SKL (PTS1) luminal import while PEX3-YFP membrane import is unaffected.
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LONP2 silencing does not induce pexophagy (no increase in LC3/p62 peroxisomal puncta), distinguishing peroxisomal proteotoxic stress from mitophagy-like turnover.
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LONP2 loss leads to cholesterol trapping in endolysosomes, INSIG1 downregulation, sphingomyelin/ceramide upregulation, repression of retinoic acid signaling (CRABP2 loss), and cell-type-specific ISR activation; all phenotypes are rescued by siRNA-resistant LONP2 cDNA.
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Lon peptidases function dually as ATP-dependent proteases and chaperones; loss-of-LONP2 protein aggregates in fungi establish the chaperone activity in vivo.
Depletion of LONP2 unmasks differential requirements for peroxisomal function between cell types and in cholesterol metabolism.
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LONP2 silencing impairs peroxisomal luminal (PTS1/CFP-SKL) protein import while membrane protein import (PEX3-YFP) is unaffected
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LONP2 substrate TYSND1 self-cleavage products accumulate upon LONP2 depletion, while ACOX1 processing is initially preserved
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LONP2 knockdown reduces peroxisome number and produces enlarged, elongated peroxisomes without inducing pexophagy
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LONP2 functions as both a chaperone and ATP-dependent protease in peroxisomes