LONP2 (Lon Peptidase 2, Peroxisomal) – Function, Processes, and Localization OpenAI o3-deep-research-2025-06-26 127 citations 2025-11-03T21:39:43.922740

LONP2 (Lon Peptidase 2, Peroxisomal) – Function, Processes, and Localization

Gene and Protein Overview

LONP2 encodes the human peroxisomal Lon protease, an ATP-dependent protease of the Lon family that localizes to the peroxisome matrix (www.ncbi.nlm.nih.gov). It is a paralog of the mitochondrial Lon protease (LONP1), arising from an early gene duplication retained from bacterial ancestors (biologydirect.biomedcentral.com). LONP2 is a AAA+ serine protease composed of distinct domains: an N-terminal “Lon N” domain for substrate recognition, a central ATPase (AAA+) domain that harnesses ATP hydrolysis, and a C-terminal peptidase domain containing the catalytic serine (www.ncbi.nlm.nih.gov). In its longer isoforms, LONP2 carries a peroxisome targeting signal type 1 (PTS1) tripeptide at the extreme C-terminus, ensuring import into the peroxisomal lumen (www.ncbi.nlm.nih.gov). Like other Lon proteases, LONP2 assembles into a multimeric ring (heptameric in fungi) which unfolds and translocates substrate polypeptides into its proteolytic core (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). This protein is expressed in most human tissues (notably high in metabolically active organs like liver and thyroid) consistent with the ubiquitous presence of peroxisomes (www.ncbi.nlm.nih.gov).

Enzymatic Function and Substrate Specificity

LONP2’s primary function is quality-control proteolysis: it selectively recognizes and degrades misfolded, damaged, or unassembled proteins within the peroxisomal matrix (www.genecards.org) (pmc.ncbi.nlm.nih.gov). Biochemically, it is an ATP-dependent serine protease, meaning ATP binding/hydrolysis is required for efficient protein degradation and a serine residue acts in its catalytic center. Experimental studies have demonstrated this mechanism directly – isolated peroxisomal LONP2 can rapidly digest model unfolded substrates (like casein) only in the presence of ATP (pmc.ncbi.nlm.nih.gov). Mutating the enzyme’s active-site serine abolishes its proteolytic activity, confirming that catalysis depends on this residue (pmc.ncbi.nlm.nih.gov). Thus, LONP2 uses ATP to drive conformational changes and substrate unfolding (as seen with mitochondrial Lon), allowing it to thread substrates into the protease chamber for degradation (pmc.ncbi.nlm.nih.gov).

LONP2 is often described as “dual-function” – a protease and a chaperone (pmc.ncbi.nlm.nih.gov). In addition to outright degradation of polypeptides, it can bind and stabilize unfolded proteins to prevent aggregation, acting in a chaperone-like capacity (pmc.ncbi.nlm.nih.gov). This was shown in fungal models where LONP2 (called Pln in yeast) was able to refold or hold substrates in vitro, and its loss led to accumulation of insoluble protein aggregates in peroxisomes (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). These findings indicate LONP2 can either refold stressed proteins or commit them to degradation, thereby maintaining a healthy folding environment in the organelle.

Substrate specificity of LONP2 appears to target proteins that are abnormal or no longer functional. It does not generally destroy native, functional enzymes, but rather “selectively digests unfolded or oxidatively damaged proteins” (pmc.ncbi.nlm.nih.gov). A prime example is catalase: in fungi, oxidatively damaged catalase-peroxidase (a peroxisomal enzyme prone to oxidative inactivation) was shown to be a LONP2 substrate, whereas the native (undamaged) catalase was spared (pmc.ncbi.nlm.nih.gov). Cells lacking LONP2 accumulate high levels of catalase-peroxidase protein that is aggregated and enzymatically inactive (pmc.ncbi.nlm.nih.gov), demonstrating that LONP2 normally removes the oxidized forms to prevent such aggregation. Another well-characterized substrate is TYSND1, a peroxisomal matrix protease. TYSND1 (trypsin domain-containing protease 1) undergoes an auto-proteolysis to generate 45 kDa and 15 kDa fragments, and LONP2 recognizes and degrades these TYSND1 fragments (pmc.ncbi.nlm.nih.gov). This was shown in mammalian cells: when LONP2 is knocked down, the cleaved fragments of TYSND1 accumulate to high levels (biologydirect.biomedcentral.com) (biologydirect.biomedcentral.com). Notably, TYSND1 itself is responsible for processing several peroxisomal enzymes – it cleaves the C-terminal targeting tripeptides of some PTS1 enzymes and removes N-terminal leader peptides from PTS2 enzymes (such as the precursor of 3-ketoacyl-CoA thiolase) (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). LONP2 thus indirectly supports these maturation steps: by degrading TYSND1 after it acts, LONP2 may reset the protease for further use or prevent an excess of its cleaved form from interfering with peroxisomal protease balance (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). In line with this, LONP2 is considered necessary for efficient processing of PTS2-containing proteins and normal peroxisomal enzyme turnover (www.genecards.org). Beyond TYSND1 and catalase, LONP2 likely targets other misfolded or surplus peroxisomal matrix proteins (e.g. import adapters or metabolic enzymes) especially if they become oxidized. In yeast and plants, additional client proteins for LONP2 have been observed, reinforcing its broad role: for instance, studies in Penicillium and Hansenula yeast identified catalase and other matrix enzymes as LONP2-dependent degradation targets (biologydirect.biomedcentral.com).

Overall, LONP2 exhibits substrate specificity in favor of “non-native” polypeptides. By binding exposed hydrophobic segments or unstructured regions (hallmarks of damaged or misfolded proteins), it discriminates defective proteins from the normal folded pool (pmc.ncbi.nlm.nih.gov). This behavior is analogous to the selectivity of cytosolic proteostasis systems (like the ubiquitin-proteasome) for aberrant proteins, but LONP2 is the dedicated protease within peroxisomes where the ubiquitin-proteasome system is absent (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov).

Localization and Peroxisomal Context

LONP2 is strictly localized to peroxisomes – specifically, the matrix (lumen) of this organelle (pmc.ncbi.nlm.nih.gov). Newly synthesized LONP2 in the cytosol is recognized and imported into peroxisomes via the PTS1 pathway, thanks to its C-terminal import signal (www.ncbi.nlm.nih.gov). The imported protein oligomerizes into a cylindrical protease complex that resides in the peroxisomal matrix, presumably free in the lumen rather than membrane-bound (similar to mitochondrial LonP1). Within peroxisomes, LONP2 is strategically positioned in an environment of high oxidative risk. Peroxisomes carry out β-oxidation of very-long-chain fatty acids and other oxidative reactions that produce hydrogen peroxide (H₂O₂) and reactive oxygen species (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Indeed, the peroxisomal core is often a site of concentrated H₂O₂ (e.g. from urate oxidase in some species) (pmc.ncbi.nlm.nih.gov). Therefore, many peroxisomal enzymes (like fatty acid oxidases and catalase) face continual oxidative stress and potential damage. LONP2’s presence in the peroxisomal lumen provides an on-site defense, immediately recognizing and removing proteins that have been inactivated by oxidation (pmc.ncbi.nlm.nih.gov). This proximity is critical – as noted by Pomatto et al. (2017), it is “logical that a proteolytic enzyme such as LonP2 would be in close proximity [to vulnerable proteins] to prevent protein aggregation,” much as mitochondrial LonP1 sits in the mitochondrial matrix to degrade oxidized respiratory chain proteins (pmc.ncbi.nlm.nih.gov). Consistently, LONP2 is relatively abundant in the peroxisome compared to other matrix proteins, highlighting its importance in such a highly oxidizing compartment (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov).

The peroxisomal localization of LONP2 is also tied to its role in protein import and processing pathways. Peroxisomes import all their matrix enzymes post-translationally from the cytosol via PEX5/PTS1 or PEX7/PTS2 pathways (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Once inside, some newly imported proteins undergo proteolytic clipping (e.g. removal of PTS2 pre-sequences or C-terminal propeptides) to become fully active. LONP2 cooperates in this maturation process: for example, the PTS2-containing thiolase requires cleavage of its N-terminal presequence by TYSND1, and LONP2 then degrades the excised presequence and any excess TYSND1 fragments (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). By clearing such peptides and inactive intermediates, LONP2 helps maintain a proper proteostasis balance that facilitates ongoing import. In fact, recent evidence indicates that if LONP2 is suppressed, peroxisomal protein import can be impaired. A 2023 study by Bailey et al. showed that silencing LONP2 led to accumulation of peroxisomal protein fragments and a failure of new proteins to import into the peroxisome lumen (biologydirect.biomedcentral.com). In LONP2-deficient cells, a fluorescent PTS1 reporter (CFP–SKL) could no longer efficiently translocate into peroxisomes even though membrane proteins still inserted normally, indicating a specific defect in matrix import likely due to a clogged or hostile luminal environment (biologydirect.biomedcentral.com) (biologydirect.biomedcentral.com). This suggests that LONP2’s activity is required to “prepare the ground” for incoming proteins, perhaps by keeping the matrix clear of aggregates or by degrading improperly imported proteins that might otherwise tie up the import machinery.

Role in Peroxisomal Homeostasis and Metabolic Pathways

LONP2 is now recognized as a key protector of peroxisomal homeostasis. By continuously eliminating damaged proteins, LONP2 prevents the formation of protein aggregates that could disrupt organelle function (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). This role is especially crucial in the face of reactive oxygen species generated inside peroxisomes. Pomatto et al. note that Lon protease–mediated degradation of oxidized proteins is “a vital mechanism to maintain protein homeostasis within the peroxisome,” providing a critical defense against the accumulation of oxidative damage (pmc.ncbi.nlm.nih.gov). If LONP2 is lacking or overwhelmed, peroxisomes swiftly lose functional capacity. Experiments in yeast and fungi have dramatically illustrated this: deleting the peroxisomal Lon gene in yeast leads to elevated levels of ROS, protein aggregates inside peroxisomes, and even increased DNA damage in the cell (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov) (likely because unchecked peroxisomal oxidation by-products can damage nuclear or mitochondrial DNA). These Lon-deficient peroxisomes often become enlarged and increase in number – a probable compensation attempt by the cell to dilute or handle the proteostatic stress (pmc.ncbi.nlm.nih.gov). In Penicillium chrysogenum lacking Lon, researchers observed significantly enlarged peroxisomes filled with electron-dense inclusion bodies of aggregated proteins (mostly oxidized catalase) (pmc.ncbi.nlm.nih.gov). Those mutant cells also showed reduced peroxisomal enzyme activities, despite elevated protein levels, consistent with many enzymes being present in a non-functional, aggregated state (pmc.ncbi.nlm.nih.gov).

Coordination with pexophagy – the autophagic degradation of peroxisomes – is another important aspect of LONP2’s role. Under normal conditions, LONP2 handles routine cleanup of damaged proteins internally; however, if damage accumulates beyond a threshold, entire peroxisomes may be removed by selective autophagy. Studies in yeast underscore this relationship: loss of LONP2 alone has modest growth effects, but simultaneous loss of LONP2 and the key autophagy gene ATG1 is highly detrimental (pmc.ncbi.nlm.nih.gov). Aksam et al. (2007) showed that a double knockout of the peroxisomal Lon protease gene (pln) and atg1 in yeast led to synergistic lethality – cells could not survive without both the protease-based quality control and the backup autophagy system (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). In these double mutants, irreparable protein damage simply accumulates: peroxisomes grew larger and more numerous (unable to be turned over), and protein aggregates built up unchecked (pmc.ncbi.nlm.nih.gov). This indicates that LONP2 and pexophagy together constitute a two-tiered proteostasis system for peroxisomes (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). LONP2 handles the first line of defense, degrading individual damaged proteins as they arise, whereas pexophagy provides a rescue pathway if an entire organelle becomes too damaged to repair. Consistently, in cells with LONP2 knocked down, there are signs of peroxisomal stress but not immediate activation of autophagy: 6-day LONP2 silencing did not significantly induce pexophagy or general autophagy markers (biologydirect.biomedcentral.com), suggesting that peroxisomes remained intact and were not being rapidly cleared. Instead, the cell activates other stress responses (discussed below) while presumably attempting to cope or wait for longer-term solutions. If the stress were prolonged or acute enough, pexophagy would likely kick in. This cooperative interaction underlines LONP2’s importance – it delays or prevents the need for destructive solutions by continually rejuvenating peroxisomes at the protein level.

Importantly, LONP2’s activity has direct implications for metabolic pathways housed in peroxisomes, especially fatty acid β-oxidation. Peroxisomes are crucial for breaking down very-long-chain fatty acids (VLCFAs) and branched-chain lipids, which are then shuttled to mitochondria for completion of oxidation (biologydirect.biomedcentral.com). Many enzymes of the β-oxidation cycle reside in the peroxisomal matrix (e.g. acyl-CoA oxidase 1 – ACOX1, the D-bifunctional enzyme, thiolase). The proper turnover and maturation of these enzymes are partly governed by TYSND1 and LONP2. Evidence shows that disrupting LONP2 can hamper peroxisomal β-oxidation. Okumoto et al. (2011) reported that siRNA knockdown of LONP2 (referred to as PsLon) in cultured cells caused a measurable decrease in VLCFA β-oxidation flux (pmc.ncbi.nlm.nih.gov). Specifically, the rate of peroxisomal oxidation of a very-long-chain fatty acid substrate was partially reduced when LONP2 was silenced (and significantly reduced when TYSND1 was silenced) (pmc.ncbi.nlm.nih.gov). This partial defect in LONP2 knockdown cells likely results from the accumulation of uncleared TYSND1 fragments and possibly a less efficient processing of matrix enzymes. In the same study, knockdown of TYSND1 caused accumulation of multiple β-oxidation enzymes in their larger, unprocessed (precursor) forms (pmc.ncbi.nlm.nih.gov), which severely curtailed β-oxidation activity. LONP2 knockdown did not cause such precursor accumulation (consistent with LONP2 not directly processing those enzymes), but it did allow buildup of TYSND1 fragments (pmc.ncbi.nlm.nih.gov). The data suggest a model wherein TYSND1 and LONP2 cooperatively regulate the fatty acid β-oxidation pathway: TYSND1 activates enzymes by cleaving them, and LONP2 then degrades TYSND1’s by-products and possibly inactivates TYSND1 itself when appropriate, to fine-tune protease levels (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). In this way, LONP2 indirectly “may regulate peroxisomal fatty acid β-oxidation through degradation of the self-processed forms of TYSND1” (www.genecards.org). Supporting this, an earlier rat study identified Lon protease in liver peroxisomes but noted its substrates “had yet to be defined” (pmc.ncbi.nlm.nih.gov). Okumoto’s work filled that gap by defining TYSND1 (and by extension the enzymes TYSND1 processes, like ACOX1) as part of LONP2’s substrate network.

Beyond fatty acid metabolism, perturbation of LONP2 affects other metabolic and signaling pathways linked to peroxisome function. Peroxisomes are involved in biosynthesis of bile acids, ether phospholipids (plasmalogens), and in reactive oxygen signaling, among other roles (biologydirect.biomedcentral.com) (biologydirect.biomedcentral.com). A striking recent finding is that LONP2 depletion can influence cellular lipid trafficking and signaling. In the 2023 study by Bailey et al., LONP2 knockdown in mammalian cells led to cholesterol accumulation in endosomal/lysosomal compartments (biologydirect.biomedcentral.com). This aligns with emerging evidence that peroxisomes facilitate cholesterol efflux from lysosomes (for example, through membrane contacts) (biologydirect.biomedcentral.com). When peroxisomal proteostasis is upset by LONP2 loss, cholesterol appears to get “stuck” in late endosomes/lysosomes, highlighting a previously underappreciated link between peroxisomal health and cholesterol homeostasis (biologydirect.biomedcentral.com). The same study also found that retinoic acid signaling pathways were down-regulated in LONP2-deficient cells, and sphingolipid levels were up-regulated (biologydirect.biomedcentral.com). Retinoic acid (a derivative of vitamin A) is partly metabolized in peroxisomes, so a dysfunction in peroxisomes could blunt RA signaling by altering RA availability or turnover. Increased sphingolipids might reflect a stress response or compensatory change in membrane composition when cholesterol handling is impaired. Together, these data indicate that peroxisomal stress caused by LONP2 loss can ripple out to broader cellular metabolism, affecting lipid distribution and signaling networks (biologydirect.biomedcentral.com) (biologydirect.biomedcentral.com).

Another major consequence of LONP2 dysfunction is the activation of cellular stress responses. When misfolded proteins accumulate in an organelle, cells often trigger signaling pathways to restore homeostasis (e.g. the unfolded protein response in ER or mitochondria). A parallel is now observed for peroxisomes: LONP2 silencing elicits an integrated stress response (ISR) in certain contexts. Specifically, in COS-7 cells (monkey kidney cells), loss of LONP2 led to a strong phosphorylation of eIF2α and upregulation of genes involved in stress and ribosome biogenesis, hallmark features of the ISR (biologydirect.biomedcentral.com) (biologydirect.biomedcentral.com). This suggests that “peroxisomal proteotoxic stress” (accumulation of unfolded proteins in peroxisomes due to LONP2 impairment) can communicate with the cytoplasm/nucleus to slow down protein synthesis and adjust gene expression. Interestingly, the stress response was somewhat cell-type-specific: COS-7 cells showed a robust ISR, whereas human U2OS cells (an osteosarcoma line) had a more muted ISR, though both cell types shared some responses (like the lipid changes mentioned) (biologydirect.biomedcentral.com) (biologydirect.biomedcentral.com). Both cell types, however, engaged transcriptional changes rather than immediately resorting to wholesale peroxisome degradation, indicating the cell attempts to mitigate the protein-folding stress by altering metabolism and gene expression when LONP2 is deficient.

Biological and Clinical Significance

Considering its fundamental role, LONP2 is crucial for the longevity and adaptability of peroxisomes. Some expert reviews have highlighted Lon proteases as critical “aging guardians” of organelle function. The mitochondrial Lon (LonP1) has long been known to decline with age and to be important for handling oxidative stress in aging cells (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). By analogy, peroxisomal LonP2 is thought to protect cells from age-related damage: peroxisomes in older organisms often show functional decline, and accumulation of oxidized peroxisomal proteins could contribute to cellular aging if not counteracted (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Indeed, peroxisomal dysfunction has been associated with age-related diseases (neurodegeneration, metabolic syndrome), and maintaining peroxisomal proteostasis is proposed to be a component of “healthy aging” (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). While direct studies of LonP2 in aging are still emerging, its role in preventing oxidative protein damage places it at the heart of preserving peroxisomal function over time (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). For example, in rodent models of peroxisome stress, young animals show higher LonP2 levels/activity compared to older ones (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov), hinting that LonP2 may diminish with age similarly to LonP1. If so, boosting LonP2 function might be a future avenue to mitigate age-related peroxisomal defects.

From a clinical perspective, genetic disruption of LONP2 in humans is rare but informative. Until recently, no classic peroxisomal biogenesis disorder was linked to LONP2, likely because peroxisomes can form normally and perform many functions even if proteostasis is suboptimal. However, in 2021 a new autosomal dominant neurodevelopmental disorder called Buratti-Harel Syndrome (BURHAS) was attributed to de novo mutations in LONP2 (www.malacards.org) (www.malacards.org). This syndrome is characterized by infantile hypotonia, delayed motor and speech milestones, mild to moderate intellectual disability, and subtle dysmorphic features (www.malacards.org). Notably, it is relatively mild compared to classical peroxisomal disorders (patients survive to childhood and can attend special schooling) (www.malacards.org). The causative LONP2 variants are heterozygous, suggesting a dominant-negative effect or haploinsufficiency. The fact that partial loss of LONP2 leads to neurological development issues underscores the enzyme’s importance in certain tissues (potentially the brain). It implies that peroxisomal protein quality control is especially vital for neuronal cells, which are highly sensitive to metabolic and oxidative imbalances. Aside from this rare syndrome, LONP2 has also been implicated as a gene of interest in cancer genomics (e.g. a correlation with bladder cancer in some datasets) (www.genecards.org), though such associations are still preliminary. In cell models, LONP2 loss did increase oxidative stress in mitochondria (at least in some cell types) (biologydirect.biomedcentral.com) and altered lipid signaling, which could conceivably contribute to pathologies if chronic. Nonetheless, no common diseases have yet been directly tied to LONP2 dysfunction, and Buratti-Harel syndrome remains the clearest example of its impact in humans.

In summary, LONP2 is an essential proteolytic guardian of the peroxisome. It catalyzes the ATP-dependent degradation of aberrant proteins in the peroxisomal matrix, with a substrate preference for oxidized or misfolded polypeptides (www.genecards.org) (pmc.ncbi.nlm.nih.gov). Through this activity (and auxiliary chaperone functions), LONP2 preserves the functional proteome of peroxisomes, enabling these organelles to carry out vital metabolic processes like fatty acid β-oxidation and peroxisomal ROS detoxification (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). It works in concert with the peroxisome-specific protease TYSND1 – together, these two proteases orchestrate the maturation and turnover of key enzymes, thereby regulating metabolic flux through peroxisomal pathways (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). LONP2’s importance is further highlighted by cellular stress responses that emerge when it is absent: peroxisome morphology changes, import mechanisms falter, and stress signals (like the ISR) activate to compensate (biologydirect.biomedcentral.com) (biologydirect.biomedcentral.com). By preventing toxic protein aggregation, LONP2 also forestalls the need for wholesale organelle degradation, integrating into the cell’s broader quality control network alongside autophagy (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Given its critical role in maintaining peroxisomal health, LONP2 is increasingly a focus of research not only for understanding peroxisome biology but also for its potential links to aging and disease. As one review succinctly stated, “the peroxisome-specific Lon protease plays a major role in maintaining peroxisomal protein homeostasis” and provides a crucial mechanism to avoid oxidative damage accumulation inside the organelle (pmc.ncbi.nlm.nih.gov). This protective function of LONP2 ultimately supports the versatility and longevity of peroxisomes, ensuring they can meet the cell’s metabolic and signaling needs without succumbing to the very oxidative pressures they generate.

References:

  1. Pomatto, L.C.D., et al. (2017). The peroxisomal Lon protease LonP2 in aging and disease: functions and comparisons with mitochondrial Lon protease LonP1. Biol. Rev. 92(2):739–753 (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov).

  2. Bartoszewska, M., et al. (2012). Peroxisomal proteostasis involves a Lon family protein that functions as protease and chaperone. J. Biol. Chem. 287(33):27380–27395 (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov).

  3. Okumoto, K., et al. (2011). Two proteases, trypsin domain–containing 1 (Tysnd1) and peroxisomal Lon protease (PsLon), cooperatively regulate fatty acid β-oxidation in the peroxisomal matrix. J. Biol. Chem. 286(52):44367–44379 (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov).

  4. Bailey, L.J., et al. (2023). Depletion of LONP2 unmasks differential requirements for peroxisomal function between cell types and in cholesterol metabolism. Biology Direct 18:60 (biologydirect.biomedcentral.com) (biologydirect.biomedcentral.com).

  5. NCBI Gene ID: 83752 (LONP2) – Gene Summary (Updated Jan 2017) (www.ncbi.nlm.nih.gov).

  6. UniProtKB entry Q86WA8 (LONP2_HUMAN) – Swiss-Prot reviewed protein, Lon protease 2 (www.genecards.org) (www.genecards.org).

  7. Aksam, E.B., et al. (2007). A peroxisomal Lon protease and peroxisome degradation by autophagy play key roles in vitality of Hansenula polymorpha. Autophagy 3(2):96–105 (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov).

  8. GeneCards entry for LONP2 (Lon Peptidase 2, Peroxisomal) – Summary of function and associated pathways (www.genecards.org) (www.genecards.org).

  9. MalaCards: Buratti-Harel Syndrome – OMIM summary of clinical features (Buratti et al., 2021) (www.malacards.org) (www.malacards.org).

Citations

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  13. AnnotationURLCitation(end_index=4074, start_index=3903, title='Peroxisomal Proteostasis Involves a Lon Family Protein That Functions as Protease and Chaperone - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3431691/#:~:text=Results%3A%20Pln%20is%20an%20ATP,peroxisomes%20that%20compromise%20organelle%20function')
  14. AnnotationURLCitation(end_index=4404, start_index=4233, title='Peroxisomal Proteostasis Involves a Lon Family Protein That Functions as Protease and Chaperone - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3431691/#:~:text=Results%3A%20Pln%20is%20an%20ATP,peroxisomes%20that%20compromise%20organelle%20function')
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  16. AnnotationURLCitation(end_index=4907, start_index=4752, title='Peroxisomal Proteostasis Involves a Lon Family Protein That Functions as Protease and Chaperone - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3431691/#:~:text=In%20cells%20of%20a%20PLN,Pln%20protease%20and%20chaperone%20activities')
  17. AnnotationURLCitation(end_index=5431, start_index=5318, title='Peroxisomal Proteostasis Involves a Lon Family Protein That Functions as Protease and Chaperone - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3431691/#:~:text=various%20species%20%28Pln%29')
  18. AnnotationURLCitation(end_index=5812, start_index=5657, title='Peroxisomal Proteostasis Involves a Lon Family Protein That Functions as Protease and Chaperone - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3431691/#:~:text=In%20cells%20of%20a%20PLN,Pln%20protease%20and%20chaperone%20activities')
  19. AnnotationURLCitation(end_index=6089, start_index=5934, title='Peroxisomal Proteostasis Involves a Lon Family Protein That Functions as Protease and Chaperone - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3431691/#:~:text=In%20cells%20of%20a%20PLN,Pln%20protease%20and%20chaperone%20activities')
  20. AnnotationURLCitation(end_index=6596, start_index=6442, title='Two Proteases, Trypsin Domain-containing 1 (Tysnd1) and Peroxisomal Lon Protease (PsLon), Cooperatively Regulate Fatty Acid β-Oxidation in Peroxisomal Matrix - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3247999/#:~:text=Results%3A%20Tysnd1%20inactivates%20its%20protease,oxidation%20enzymes')
  21. AnnotationURLCitation(end_index=6889, start_index=6719, title='Depletion of LONP2 unmasks differential requirements for peroxisomal function between cell types and in cholesterol metabolism | Biology Direct | Full Text', type='url_citation', url='https://biologydirect.biomedcentral.com/articles/10.1186/s13062-023-00416-3#:~:text=COS,LONP2%20inside%20peroxisomes%20was%20impaired')
  22. AnnotationURLCitation(end_index=7098, start_index=6890, title='Depletion of LONP2 unmasks differential requirements for peroxisomal function between cell types and in cholesterol metabolism | Biology Direct | Full Text', type='url_citation', url='https://biologydirect.biomedcentral.com/articles/10.1186/s13062-023-00416-3#:~:text=revealed%20an%20accumulation%20of%20the,accumulation%20of%20these%20autocleaved%20forms')
  23. AnnotationURLCitation(end_index=7539, start_index=7364, title='Two Proteases, Trypsin Domain-containing 1 (Tysnd1) and Peroxisomal Lon Protease (PsLon), Cooperatively Regulate Fatty Acid β-Oxidation in Peroxisomal Matrix - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3247999/#:~:text=the%20peroxisomal%20matrix%20remain%20largely,which%20were%20preferentially%20degraded%20by')
  24. AnnotationURLCitation(end_index=7658, start_index=7540, title='Two Proteases, Trypsin Domain-containing 1 (Tysnd1) and Peroxisomal Lon Protease (PsLon), Cooperatively Regulate Fatty Acid β-Oxidation in Peroxisomal Matrix - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3247999/#:~:text=CoA,have%20yet%20to%20be%20defined')
  25. AnnotationURLCitation(end_index=8041, start_index=7887, title='Two Proteases, Trypsin Domain-containing 1 (Tysnd1) and Peroxisomal Lon Protease (PsLon), Cooperatively Regulate Fatty Acid β-Oxidation in Peroxisomal Matrix - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3247999/#:~:text=Results%3A%20Tysnd1%20inactivates%20its%20protease,oxidation%20enzymes')
  26. AnnotationURLCitation(end_index=8207, start_index=8042, title='Two Proteases, Trypsin Domain-containing 1 (Tysnd1) and Peroxisomal Lon Protease (PsLon), Cooperatively Regulate Fatty Acid β-Oxidation in Peroxisomal Matrix - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3247999/#:~:text=accumulation%20of%20endogenous%20%CE%B2,Tysnd1%20cleavage%20products%20by%20PsLon')
  27. AnnotationURLCitation(end_index=8472, start_index=8354, title='LONP2 Gene - GeneCards | LONP2 Protein | LONP2 Antibody', type='url_citation', url='https://www.genecards.org/cgi-bin/carddisp.pl?gene=LONP2#:~:text=ATP,%28%20LONP2_HUMAN%2CQ86WA8')
  28. AnnotationURLCitation(end_index=9133, start_index=8917, title='Depletion of LONP2 unmasks differential requirements for peroxisomal function between cell types and in cholesterol metabolism | Biology Direct | Full Text', type='url_citation', url='https://biologydirect.biomedcentral.com/articles/10.1186/s13062-023-00416-3#:~:text=directly%20investigated%20the%20biochemistry%20and,and%20other%20clients%20including%20catalase')
  29. AnnotationURLCitation(end_index=9556, start_index=9401, title='Peroxisomal Proteostasis Involves a Lon Family Protein That Functions as Protease and Chaperone - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3431691/#:~:text=In%20cells%20of%20a%20PLN,Pln%20protease%20and%20chaperone%20activities')
  30. AnnotationURLCitation(end_index=9966, start_index=9800, title='The peroxisomal Lon protease LonP2 in aging and disease: functions and comparisons with mitochondrial Lon protease LonP1 - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC5159316/#:~:text=degrades%20proteins%20damaged%20by%20reactive,functional%20enzyme%2C%20is%20highly')
  31. AnnotationURLCitation(end_index=10128, start_index=9967, title='The peroxisomal Lon protease LonP2 in aging and disease: functions and comparisons with mitochondrial Lon protease LonP1 - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC5159316/#:~:text=to%20the%20mitochondrial%20isoform%20of,role%20in%20fatty%20acid%20metabolism')
  32. AnnotationURLCitation(end_index=10419, start_index=10274, title='Two Proteases, Trypsin Domain-containing 1 (Tysnd1) and Peroxisomal Lon Protease (PsLon), Cooperatively Regulate Fatty Acid β-Oxidation in Peroxisomal Matrix - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3247999/#:~:text=the%20peroxisomal%20matrix%20remain%20largely,conversion%20of')
  33. AnnotationURLCitation(end_index=10734, start_index=10565, title='LONP2 lon peptidase 2, peroxisomal [Homo sapiens (human)] - Gene - NCBI', type='url_citation', url='https://www.ncbi.nlm.nih.gov/gene/83752#:~:text=In%20human%2C%20peroxisomes%20function%20primarily,terminal%20peroxisome%20targeting%20sequence')
  34. AnnotationURLCitation(end_index=11368, start_index=11197, title='The peroxisomal Lon protease LonP2 in aging and disease: functions and comparisons with mitochondrial Lon protease LonP1 - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC5159316/#:~:text=Peroxisomes%20are%20ubiquitous%20eukaryotic%20organelles,in%20relation%20to%20oxidative')
  35. AnnotationURLCitation(end_index=11531, start_index=11369, title='The peroxisomal Lon protease LonP2 in aging and disease: functions and comparisons with mitochondrial Lon protease LonP1 - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC5159316/#:~:text=double%20membrane%2C%20peroxisomes%20possess%20a,20%20Nordgren%20%26%20Fransen')
  36. AnnotationURLCitation(end_index=11802, start_index=11641, title='The peroxisomal Lon protease LonP2 in aging and disease: functions and comparisons with mitochondrial Lon protease LonP1 - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC5159316/#:~:text=The%20peroxisome%20is%20an%20abundant,enzymes%2C%20such%20as%20catalase%20and')
  37. AnnotationURLCitation(end_index=12192, start_index=12095, title='The peroxisomal Lon protease LonP2 in aging and disease: functions and comparisons with mitochondrial Lon protease LonP1 - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC5159316/#:~:text=1995%20%29,21')
  38. AnnotationURLCitation(end_index=12653, start_index=12509, title='The peroxisomal Lon protease LonP2 in aging and disease: functions and comparisons with mitochondrial Lon protease LonP1 - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC5159316/#:~:text=to%20protein%20damage,a%20similarity%20shared%20with%20LonP1')
  39. AnnotationURLCitation(end_index=12966, start_index=12822, title='The peroxisomal Lon protease LonP2 in aging and disease: functions and comparisons with mitochondrial Lon protease LonP1 - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC5159316/#:~:text=to%20protein%20damage,a%20similarity%20shared%20with%20LonP1')
  40. AnnotationURLCitation(end_index=13138, start_index=12967, title='The peroxisomal Lon protease LonP2 in aging and disease: functions and comparisons with mitochondrial Lon protease LonP1 - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC5159316/#:~:text=Furthermore%2C%20the%20relative%20abundance%20of,a%20similarity%20shared%20with%20LonP1')
  41. AnnotationURLCitation(end_index=13511, start_index=13369, title='Two Proteases, Trypsin Domain-containing 1 (Tysnd1) and Peroxisomal Lon Protease (PsLon), Cooperatively Regulate Fatty Acid β-Oxidation in Peroxisomal Matrix - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3247999/#:~:text=The%20peroxisome%20is%20an%20organelle,Extensive%20studies')
  42. AnnotationURLCitation(end_index=13636, start_index=13512, title='Two Proteases, Trypsin Domain-containing 1 (Tysnd1) and Peroxisomal Lon Protease (PsLon), Cooperatively Regulate Fatty Acid β-Oxidation in Peroxisomal Matrix - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3247999/#:~:text=reviews%2C%20see%20Refs,16%20%2C%20%2022')
  43. AnnotationURLCitation(end_index=14176, start_index=14022, title='Two Proteases, Trypsin Domain-containing 1 (Tysnd1) and Peroxisomal Lon Protease (PsLon), Cooperatively Regulate Fatty Acid β-Oxidation in Peroxisomal Matrix - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3247999/#:~:text=Results%3A%20Tysnd1%20inactivates%20its%20protease,oxidation%20enzymes')
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  45. AnnotationURLCitation(end_index=14948, start_index=14777, title='Depletion of LONP2 unmasks differential requirements for peroxisomal function between cell types and in cholesterol metabolism | Biology Direct | Full Text', type='url_citation', url='https://biologydirect.biomedcentral.com/articles/10.1186/s13062-023-00416-3#:~:text=%28PEX3,into%20the%20peroxisomal%20lumen%20without')
  46. AnnotationURLCitation(end_index=15398, start_index=15227, title='Depletion of LONP2 unmasks differential requirements for peroxisomal function between cell types and in cholesterol metabolism | Biology Direct | Full Text', type='url_citation', url='https://biologydirect.biomedcentral.com/articles/10.1186/s13062-023-00416-3#:~:text=%28PEX3,into%20the%20peroxisomal%20lumen%20without')
  47. AnnotationURLCitation(end_index=15606, start_index=15399, title='Depletion of LONP2 unmasks differential requirements for peroxisomal function between cell types and in cholesterol metabolism | Biology Direct | Full Text', type='url_citation', url='https://biologydirect.biomedcentral.com/articles/10.1186/s13062-023-00416-3#:~:text=leads%20to%20alterations%20in%20proteolysis,into%20the%20peroxisomal%20lumen%20without')
  48. AnnotationURLCitation(end_index=16216, start_index=16123, title='The peroxisomal Lon protease LonP2 in aging and disease: functions and comparisons with mitochondrial Lon protease LonP1 - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC5159316/#:~:text=%282H_,21')
  49. AnnotationURLCitation(end_index=16372, start_index=16217, title='Peroxisomal Proteostasis Involves a Lon Family Protein That Functions as Protease and Chaperone - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3431691/#:~:text=In%20cells%20of%20a%20PLN,Pln%20protease%20and%20chaperone%20activities')
  50. AnnotationURLCitation(end_index=16802, start_index=16709, title='The peroxisomal Lon protease LonP2 in aging and disease: functions and comparisons with mitochondrial Lon protease LonP1 - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC5159316/#:~:text=%282H_,21')
  51. AnnotationURLCitation(end_index=17280, start_index=17118, title='The peroxisomal Lon protease LonP2 in aging and disease: functions and comparisons with mitochondrial Lon protease LonP1 - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC5159316/#:~:text=peroxisomes%20and%20mitochondria%20,lacking%20LonP2%20showed%20increased%20DNA')
  52. AnnotationURLCitation(end_index=17442, start_index=17281, title='The peroxisomal Lon protease LonP2 in aging and disease: functions and comparisons with mitochondrial Lon protease LonP1 - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC5159316/#:~:text=match%20at%20L449%20damage%20,demonstrates%20the%20connection%20between%20the')
  53. AnnotationURLCitation(end_index=17869, start_index=17712, title='The peroxisomal Lon protease LonP2 in aging and disease: functions and comparisons with mitochondrial Lon protease LonP1 - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC5159316/#:~:text=In%20addition%2C%20pln%20and%20pln,This%20downstream%20effect%20resulting')
  54. AnnotationURLCitation(end_index=18222, start_index=18067, title='Peroxisomal Proteostasis Involves a Lon Family Protein That Functions as Protease and Chaperone - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3431691/#:~:text=In%20cells%20of%20a%20PLN,Pln%20protease%20and%20chaperone%20activities')
  55. AnnotationURLCitation(end_index=18563, start_index=18408, title='Peroxisomal Proteostasis Involves a Lon Family Protein That Functions as Protease and Chaperone - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3431691/#:~:text=In%20cells%20of%20a%20PLN,Pln%20protease%20and%20chaperone%20activities')
  56. AnnotationURLCitation(end_index=19236, start_index=19066, title='The peroxisomal Lon protease LonP2 in aging and disease: functions and comparisons with mitochondrial Lon protease LonP1 - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC5159316/#:~:text=deleting%20the%20homolog%20for%20peroxisomal,degradation%20rate%20of%20Lon%2C%20making')
  57. AnnotationURLCitation(end_index=19657, start_index=19490, title='The peroxisomal Lon protease LonP2 in aging and disease: functions and comparisons with mitochondrial Lon protease LonP1 - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC5159316/#:~:text=deleting%20the%20homolog%20for%20peroxisomal,accumulation%20of%20high%20levels%20of')
  58. AnnotationURLCitation(end_index=19825, start_index=19658, title='The peroxisomal Lon protease LonP2 in aging and disease: functions and comparisons with mitochondrial Lon protease LonP1 - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC5159316/#:~:text=reactive%20oxygen%20species%2C%20whereas%20the,and%20inability%20to%20degrade%20the')
  59. AnnotationURLCitation(end_index=20168, start_index=20011, title='The peroxisomal Lon protease LonP2 in aging and disease: functions and comparisons with mitochondrial Lon protease LonP1 - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC5159316/#:~:text=In%20addition%2C%20pln%20and%20pln,This%20downstream%20effect%20resulting')
  60. AnnotationURLCitation(end_index=20441, start_index=20283, title='The peroxisomal Lon protease LonP2 in aging and disease: functions and comparisons with mitochondrial Lon protease LonP1 - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC5159316/#:~:text=protein%20damage%20may%20exceed%20the,and%20inability%20to%20degrade%20the')
  61. AnnotationURLCitation(end_index=20572, start_index=20442, title='The peroxisomal Lon protease LonP2 in aging and disease: functions and comparisons with mitochondrial Lon protease LonP1 - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC5159316/#:~:text=peroxisome%20when%20the%20damage%20became,2007')
  62. AnnotationURLCitation(end_index=21174, start_index=20997, title='Depletion of LONP2 unmasks differential requirements for peroxisomal function between cell types and in cholesterol metabolism | Biology Direct | Full Text', type='url_citation', url='https://biologydirect.biomedcentral.com/articles/10.1186/s13062-023-00416-3#:~:text=or%20mitophagy%20,media%2C%20starving%20the%20cells%20of')
  63. AnnotationURLCitation(end_index=22140, start_index=21972, title='Depletion of LONP2 unmasks differential requirements for peroxisomal function between cell types and in cholesterol metabolism | Biology Direct | Full Text', type='url_citation', url='https://biologydirect.biomedcentral.com/articles/10.1186/s13062-023-00416-3#:~:text=catalase,function%20of%20peroxisomes%20is%20the')
  64. AnnotationURLCitation(end_index=22748, start_index=22614, title='Two Proteases, Trypsin Domain-containing 1 (Tysnd1) and Peroxisomal Lon Protease (PsLon), Cooperatively Regulate Fatty Acid β-Oxidation in Peroxisomal Matrix - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3247999/#:~:text=the%2060,Tysnd1%20cleavage%20products%20by%20PsLon')
  65. AnnotationURLCitation(end_index=23081, start_index=22947, title='Two Proteases, Trypsin Domain-containing 1 (Tysnd1) and Peroxisomal Lon Protease (PsLon), Cooperatively Regulate Fatty Acid β-Oxidation in Peroxisomal Matrix - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3247999/#:~:text=the%2060,Tysnd1%20cleavage%20products%20by%20PsLon')
  66. AnnotationURLCitation(end_index=23532, start_index=23393, title='Two Proteases, Trypsin Domain-containing 1 (Tysnd1) and Peroxisomal Lon Protease (PsLon), Cooperatively Regulate Fatty Acid β-Oxidation in Peroxisomal Matrix - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3247999/#:~:text=proteins%20and%20cleaves%20N,oxidation%20enzymes.%20The')
  67. AnnotationURLCitation(end_index=23903, start_index=23749, title='Two Proteases, Trypsin Domain-containing 1 (Tysnd1) and Peroxisomal Lon Protease (PsLon), Cooperatively Regulate Fatty Acid β-Oxidation in Peroxisomal Matrix - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3247999/#:~:text=Results%3A%20Tysnd1%20inactivates%20its%20protease,oxidation%20enzymes')
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  70. AnnotationURLCitation(end_index=24772, start_index=24654, title='LONP2 Gene - GeneCards | LONP2 Protein | LONP2 Antibody', type='url_citation', url='https://www.genecards.org/cgi-bin/carddisp.pl?gene=LONP2#:~:text=ATP,%28%20LONP2_HUMAN%2CQ86WA8')
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  72. AnnotationURLCitation(end_index=25652, start_index=25481, title='Depletion of LONP2 unmasks differential requirements for peroxisomal function between cell types and in cholesterol metabolism | Biology Direct | Full Text', type='url_citation', url='https://biologydirect.biomedcentral.com/articles/10.1186/s13062-023-00416-3#:~:text=shorter%20lengths%2C%20they%20are%20transferred,21')
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