AIMP2 (JTV-1/p38) – Function, Interactions, and Clinical Significance OpenAI o3-deep-research-2025-06-26 122 citations 2025-12-27T17:43:20.735497

AIMP2 (JTV-1/p38) – Function, Interactions, and Clinical Significance

Gene Identity and Role in Translation

AIMP2 (ARS-interacting multi-functional protein 2, also known as JTV-1 or p38) is a human protein of 320 amino acids that serves as a non-catalytic scaffolding component of the multi-aminoacyl-tRNA synthetase complex (MSC) (www.ncbi.nlm.nih.gov) (www.nome.bio). This large complex comprises multiple aminoacyl-tRNA synthetases (eight canonical enzymes in higher eukaryotes, including the bifunctional Glu-Pro tRNA synthetase) together with three auxiliary factors (AIMP1/p43, AIMP2/p38, and AIMP3/p18) (pmc.ncbi.nlm.nih.gov). AIMP2 is required for the assembly and stability of the MSC, essentially acting as a glue that organizes the enzymes responsible for charging tRNAs during protein synthesis (www.ncbi.nlm.nih.gov) (www.antibodypedia.com). Consistent with this vital role, animal studies show that AIMP2 is indispensable: mice lacking Aimp2 die shortly after birth with severely reduced tRNA synthetase activity (www.nome.bio), underscoring its importance in maintaining the translation machinery.

Structurally, AIMP2 contains distinct domains that mediate its interactions within the complex. It has an N-terminal region that binds lysyl-tRNA synthetase (LysRS), a central segment harboring a presumed leucine-zipper motif, and a C-terminal glutathione S-transferase (GST)-like domain (pmc.ncbi.nlm.nih.gov). These domains allow AIMP2 to tether specific synthetases: for example, AIMP2’s GST-homology domain forms a dimer with the GST domain of EPRS (Glu-Pro tRNA synthetase), and together with methionyl-tRNA synthetase (MRS) and AIMP3, they assemble into a heterotetrameric subcomplex that is part of the MSC’s core architecture (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). AIMP2 also interacts with aspartyl-tRNA synthetase (AspRS) via specific loop-loop contacts between the two proteins (pmc.ncbi.nlm.nih.gov), and its N-terminal LysRS-binding motif recruits lysyl-tRNA synthetase into the complex (pmc.ncbi.nlm.nih.gov). Through these multiple attachments, AIMP2 ensures that the cohort of nine enzyme activities and the other scaffolds are optimally arranged, facilitating efficient aminoacylation of tRNAs during protein translation (www.antibodypedia.com) (pmc.ncbi.nlm.nih.gov). In summary, under normal conditions AIMP2 resides in the cytosol as an integral part of the translation apparatus, stabilizing the multisynthetase ensemble required for protein synthesis.

Stress Response and Tumor Suppressor Functions

Beyond its housekeeping role in translation, AIMP2 has critical signaling functions, especially in responses to cellular stress and regulation of cell death. AIMP2 is widely recognized as a tumor suppressor protein, and a growing body of evidence indicates that it links certain stress signals to apoptotic pathways (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Notably, AIMP2 typically exerts these effects when it dissociates from the MSC and translocates to the nucleus or other locations in response to stress stimuli (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). This release from the cytosolic complex is often triggered by phosphorylation events. For example, under genotoxic stress (DNA damage), c-Jun N-terminal kinase (JNK) phosphorylates AIMP2, causing it to detach from the MSC and migrate into the nucleus (pmc.ncbi.nlm.nih.gov). Similarly, TGF-β signaling can induce AIMP2 expression and phosphorylation at Ser-156 by p38 MAPK, promoting AIMP2’s nuclear translocation in certain contexts (e.g. lung cell differentiation) (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). In the nucleus, AIMP2 engages in multiple protein–protein interactions that promote apoptosis and inhibit proliferation.

p53 Activation in DNA Damage: One well-characterized function of AIMP2 is to stabilize and activate the tumor suppressor p53 during DNA damage responses. Upon DNA damage, liberated AIMP2 directly binds to p53 and protects it from proteasomal destruction by blocking the MDM2 ubiquitin ligase (pmc.ncbi.nlm.nih.gov). Han et al. (2008) first showed that AIMP2 (p38) can form a complex with p53, preventing MDM2-mediated ubiquitination and thereby increasing p53 levels and activity (pmc.ncbi.nlm.nih.gov). This mechanism enhances p53-dependent transcription of pro-apoptotic genes, tipping the balance toward cell cycle arrest or apoptosis in damaged cells. Cellular experiments support this role: AIMP2-deficient cells are resistant to apoptosis induced by DNA-damaging agents, whereas overexpression of AIMP2 sensitizes cells to genotoxic death signals (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Thus, AIMP2 acts as a p53 co-factor under stress conditions, explaining why reduced AIMP2 can compromise p53 function. Indeed, a haploinsufficient effect is observed in vivo: mice with only one functional Aimp2 gene show increased susceptibility to spontaneous tumors, consistent with impaired p53-mediated tumor suppression (pmc.ncbi.nlm.nih.gov). In summary, AIMP2 serves as a nuclear relay for DNA-damage signals, ensuring p53 is stabilized to eliminate cells with genomic insults.

TNF-α Pathway and Apoptosis: AIMP2 also interfaces with the extrinsic apoptosis pathway initiated by tumor necrosis factor-alpha (TNF-α). Choi et al. (2009) reported that AIMP2 enhances cellular sensitivity to TNF-α–induced death by targeting a key survival factor in the TNF pathway (pmc.ncbi.nlm.nih.gov). Specifically, AIMP2 binds to the adaptor protein TRAF2 (TNF receptor–associated factor 2) and promotes its ubiquitination and degradation via recruitment of the E3 ubiquitin ligase c-IAP1 (pmc.ncbi.nlm.nih.gov). This action removes TRAF2, which normally helps activate NF-κB and other pro-survival signals downstream of TNF receptors. In cells lacking AIMP2, TNF-α exposure results in markedly less apoptosis, indicating that TRAF2 remains intact to transmit survival signals (pmc.ncbi.nlm.nih.gov). Conversely, introducing exogenous AIMP2 restores the pro-apoptotic response to TNF-α (pmc.ncbi.nlm.nih.gov). In essence, AIMP2 acts as an apoptosis facilitator in the TNF pathway – by driving the ubiquitin-dependent turnover of TRAF2, it tilts the balance toward caspase activation and cell death (pmc.ncbi.nlm.nih.gov). This mechanism is another facet of AIMP2’s tumor-suppressive activity, as it ensures effective elimination of potentially cancerous cells in the presence of inflammatory cytokines. Notably, AIMP2 was initially identified as “p38” in the MSC, but later studies like Choi et al. showed it moonlights in TNF signaling (pubmed.ncbi.nlm.nih.gov). These findings highlight AIMP2’s broader role as a linker between the translational apparatus and cell death pathways.

Wnt/β-Catenin Signaling Regulation: Emerging research indicates AIMP2 can antagonize pro-growth signaling pathways such as Wnt/β-catenin. AIMP2 was found to interact with Dishevelled 1 (DVL1), a pivotal cytoplasmic component of Wnt signal transduction (pmc.ncbi.nlm.nih.gov). By binding DVL1, AIMP2 disrupts the formation of the DVL1–Axin complex that is normally required to inhibit the β-catenin destruction complex (pmc.ncbi.nlm.nih.gov). In one study, loss of AIMP2 led to uninhibited Wnt signaling; specifically, AIMP2^+/− mice (which express less AIMP2) showed enlarged intestinal stem cell compartments and were predisposed to intestinal tumors due to elevated Wnt/β-catenin activity (pmc.ncbi.nlm.nih.gov). Conversely, AIMP2 binding to DVL1 helped suppress β-catenin signaling, thereby restricting excessive cell proliferation in intestinal epithelium (pmc.ncbi.nlm.nih.gov). This Wnt-inhibitory function further explains AIMP2’s haploinsuppressive tumor suppression: even partial loss of AIMP2 can unleash Wnt-driven tumorigenesis (e.g. accelerating polyp formation in APC^Min/+ colon cancer models) (pmc.ncbi.nlm.nih.gov). Thus, AIMP2 plays a modulatory role in developmental signaling pathways, keeping proto-oncogenic signals like Wnt in check under normal circumstances.

c-Myc and FBP Degradation: Another critical target of AIMP2’s extratranslational activity is the c-Myc oncogene pathway. AIMP2 helps restrain c-Myc by promoting the degradation of FUBP1 (far upstream element-binding protein 1, also called FBP), which is a transcriptional activator of the MYC gene. Under growth-inhibitory signals such as TGF-β, AIMP2 gets phosphorylated (at Ser-156) and relocates to the nucleus where it partners with the HECT-domain E3 ligase Smurf2 (yonsei.elsevierpure.com) (pmc.ncbi.nlm.nih.gov). AIMP2 serves as the adaptor that brings Smurf2 to FUBP1, leading to ubiquitin-mediated proteolysis of FUBP1 (yonsei.elsevierpure.com). By removing FUBP1, AIMP2 effectively reduces c-Myc transcription, since FUBP1 normally binds the MYC promoter to enhance its expression. This pathway was elucidated by Kim et al. (2016), who showed that preventing AIMP2’s interaction with Smurf2 (through an oncogenic mutation in AIMP2) abrogated FUBP1 ubiquitination and allowed c-Myc levels to remain elevated, resulting in increased cellular transformation and tumorigenesis (yonsei.elsevierpure.com). In line with this, TGF-β stimulation was found to increase AIMP2 expression and nuclear translocation in certain cells, where AIMP2 then contributed to c-Myc downregulation and differentiation via FUBP1 degradation (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Collectively, these findings position AIMP2 as a multifaceted suppressor of oncogenic programs: it can engage ubiquitin ligases (like Smurf2 or c-IAP1) to eliminate pro-survival or pro-growth factors (such as FUBP1 and TRAF2), thereby enforcing cell cycle arrest or apoptosis. As a 2020 review succinctly noted, although AIMP2’s full spectrum of functions is still being uncovered, it “usually shows tumor-suppressive activities”, and reducing AIMP2 (for instance, in heterozygous knockout mice) leads to greater tumor susceptibility (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov).

Other Biological Roles in Neurons and Immunity

While AIMP2’s best-studied non-catalytic roles relate to tumor suppression, the protein has also been implicated in certain neurodegenerative and antiviral processes, highlighting its broad importance in cell fate decisions. In the nervous system, AIMP2 has been linked to Parkinson’s disease (PD) pathogenesis. AIMP2 was identified as a substrate of the Parkin E3 ubiquitin ligase, which is encoded by the PARK2 gene that is mutated in some familial PD (pmc.ncbi.nlm.nih.gov). Under normal conditions, Parkin ubiquitylates AIMP2 in neurons, targeting it for degradation and preventing its accumulation (pmc.ncbi.nlm.nih.gov). If Parkin is lost (as in PARK2-mutant PD patients), AIMP2 levels rise in dopaminergic neurons, with deleterious consequences. Lee et al. showed that excess AIMP2 in neurons can trigger PARP1 overactivation – AIMP2 physically interacts with poly(ADP-ribose) polymerase-1 and overactivates it, leading to accumulation of poly(ADP-ribose) polymers and a form of programmed cell death known as parthanatos (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). This mechanism contributes to progressive loss of dopamine-producing neurons in the brain. Consistently, overexpression of AIMP2 in dopaminergic cell lines causes cell death, whereas increasing Parkin or the endosomal protein VPS35 (which helps clear AIMP2 via lysosomes) can rescue cells by promoting AIMP2 degradation (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). These findings suggest that, although AIMP2’s pro-apoptotic activity may protect against cancer, it can be harmful to post-mitotic neurons if not kept in check. Interestingly, a natural splice variant of AIMP2 (termed AIMP2-DX2, discussed below) appears to counteract AIMP2-induced toxicity in neurons: this shorter variant can bind PARP1 without activating it, thereby competitively blocking the toxic AIMP2–PARP1 interaction (pmc.ncbi.nlm.nih.gov) (www.nome.bio). Experimental gene therapy in PD models has leveraged this fact – introducing AIMP2-DX2 via an adeno-associated virus vector into the brains of PD mice protected their neurons and improved motor function, essentially by using the AIMP2-DX2 protein as a “decoy” to prevent endogenous AIMP2 from overactivating PARP1 (www.nome.bio). Such findings underscore the delicate balance of AIMP2’s activity: it must be carefully regulated to allow normal cell survival, and its dysregulation is a factor in neurodegeneration.

In the immune realm, recent research (2023–2024) revealed a surprising antiviral role for AIMP2. Ren et al. (2024) discovered that AIMP2 can act as a host restriction factor against enteroviruses, including the pathogen EV71 (which causes hand, foot and mouth disease) (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). In infected cells, AIMP2 was found to bind to the viral 3D RNA polymerase and recruit the ubiquitin ligase Smurf2, paralleling its behavior in cellular signaling pathways (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). This interaction leads to polyubiquitination and proteasomal degradation of the viral polymerase, thereby inhibiting viral genome replication (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Overexpressing AIMP2 in cell culture produced a dose-dependent suppression of EV71: viral protein levels and RNA titers dropped markedly as AIMP2 levels were increased (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Moreover, the study showed that the antiviral effect was not limited to EV71 – AIMP2 similarly impeded replication of related enteroviruses (such as Coxsackievirus A16 and B1) by the same mechanism (pmc.ncbi.nlm.nih.gov). Intriguingly, enterovirus infection appears to actively downregulate AIMP2 expression, presumably as a viral counter-defense: EV71-infected cells showed a significant decrease in AIMP2 mRNA and protein over time (pmc.ncbi.nlm.nih.gov). This suggests the virus benefits from eliminating AIMP2 to evade its antiviral ubiquitination trap. The identification of AIMP2 in antiviral immunity is a striking example of a new function for this “multifunctional protein,” expanding its significance beyond the realms of translation and tumor biology. It also provides a potential avenue for therapy – boosting AIMP2 or mimicking its action might help combat certain viral infections (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). More broadly, AIMP2’s activities in disparate contexts (cancer suppression, neuronal cell death, and antiviral defense) all involve selective protein interactions and ubiquitin-mediated regulation, reinforcing the concept that AIMP2 is a versatile mediator that connects cellular stress signals to appropriate effector outcomes. As one analysis noted, AIMP2 acts as a multifaceted regulator of cell fate by targeting proteins like p53, FBP, TRAF2, and even viral enzymes for stability control (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov).

Clinical Significance and Therapeutic Developments

Genetic Disorders (HLD17): Given AIMP2’s crucial role in protein synthesis and cell viability, it is not surprising that loss-of-function mutations in this gene lead to severe human disease. Recently, biallelic mutations in AIMP2 have been linked to a rare inherited neurodevelopmental syndrome classified as hypomyelinating leukodystrophy 17 (HLD17) (www.ncbi.nlm.nih.gov). Shukla et al. (2018) first reported a nonsense mutation (c.105C>A, p.Tyr35Ter) in AIMP2 in two unrelated families; affected children exhibited profound developmental delays, microcephaly, early-onset seizures, spastic quadriplegia, and MRI evidence of leukodystrophy (defective myelination of white matter) (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). More recently, an infant from an Iranian family was found to carry a different AIMP2 nonsense variant (c.463A>T, p.Lys155Ter) in homozygous form, resulting in a similar clinical picture of progressive neurological deterioration, white-matter atrophy, severe anemia, and skeletal abnormalities (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). These cases establish that complete loss of AIMP2 function in humans is neurotoxic, likely because the multisynthetase complex cannot assemble properly in the absence of AIMP2, leading to disrupted protein synthesis particularly in the energy-demanding brain. Consistent with that, cells derived from these patients show markedly reduced aminoacyl-tRNA synthetase activities and likely heightened susceptibility to apoptosis, mirroring the phenotype of AIMP2-null mice (www.nome.bio). There is currently no cure for AIMP2-related leukodystrophy, but these findings highlight the need for early genetic diagnosis (e.g. by whole-exome sequencing) in infants with unexplained leukodystrophy (pmc.ncbi.nlm.nih.gov). Efforts are underway to explore antisense oligonucleotide (ASO) therapies that could introduce small amounts of functional AIMP2 or modulate its splicing, as a personalized strategy for families affected by this ultra-rare disorder (www.nome.bio) (www.nome.bio).

Cancer and AIMP2-DX2 Variant: In oncology, AIMP2 is attracting interest both as a biomarker and as a therapeutic target, especially because of an alternatively spliced isoform called AIMP2-DX2. AIMP2-DX2 is a splice variant missing exon 2 of the normal transcript, and it produces a truncated protein (lacking residues 36–103 of full-length AIMP2) that retains the GST-like domains but behaves in a dominant-negative manner (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Importantly, AIMP2-DX2 binds many of the same partners as full-length AIMP2 – including p53, TRAF2, and FUBP1 – but it cannot execute the tumor-suppressive functions of AIMP2 (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Instead, AIMP2-DX2 competes with the wild-type protein for binding to these targets, thereby impairing the pro-apoptotic and checkpoint activities of AIMP2. Under normal conditions, AIMP2-DX2 is barely expressed (and is often undetectable in healthy tissues) (pmc.ncbi.nlm.nih.gov). In cancers, however, this splice variant is frequently upregulated and has been identified as an oncogenic factor. It was shown that AIMP2-DX2 is highly expressed in a variety of tumors, with particularly elevated levels reported in lung cancer, colorectal and stomach cancers, pancreatic cancer, ovarian cancer, and nasopharyngeal carcinoma (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Ectopic overexpression of AIMP2-DX2 in experimental models can drive the transformation of normal cells into malignant cells, underscoring its actively tumorigenic potential (pmc.ncbi.nlm.nih.gov). Clinically, the presence of AIMP2-DX2 often correlates with worse outcomes. For instance, a 2020 study of acute myeloid leukemia (AML) patients found that 43.1% of cases had positive AIMP2-DX2 expression at diagnosis, and this subset had significantly shorter overall survival compared to AIMP2-DX2–negative patients (www.nome.bio). Likewise, analyses in solid tumors have linked a high AIMP2-DX2 to AIMP2 ratio with aggressive disease: in nasopharyngeal carcinoma, a higher DX2/full-length ratio was associated with poorer prognosis, suggesting this metric could stratify patients by risk (pmc.ncbi.nlm.nih.gov). Given these observations, AIMP2-DX2 is being actively explored as a drug target. One approach is to restore normal splicing – researchers have proposed using splice-switching antisense oligonucleotides to promote inclusion of exon 2, thereby shifting the balance back to the tumor-suppressive full-length AIMP2 (www.nome.bio) (www.nome.bio). Another strategy is to selectively destroy or inhibit the DX2 protein. High-throughput screening has identified small molecules that target AIMP2-DX2: for example, pyrimethamine (an old antimalarial drug) was found to induce ubiquitination and degradation of AIMP2-DX2 (IC_50 ≈ 0.7 μM) (www.nome.bio). A more potent investigational compound, BC-DXI-32982, disrupts the interaction between AIMP2-DX2 and mutant KRAS proteins, and it showed dose-dependent tumor growth suppression in preclinical models (IC_50 ≈ 0.18 μM) (www.nome.bio) (www.nome.bio). These agents are in preclinical development and exemplify a novel avenue of targeted therapy: by neutralizing AIMP2-DX2, they aim to unleash the natural tumor suppressor functions of AIMP2 in cancers that overexpress the splicing variant.

Prognostic and Therapeutic Biomarker: The expression status of AIMP2 (and its splice form) is also being studied as a biomarker to guide cancer treatment. Notably, a 2023 study employing multi-omics analysis of gliomas found that AIMP2 is a predictive biomarker for anti-angiogenic therapy in aggressive brain tumors (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). In recurrent glioblastoma (GBM), patients with high AIMP2 mRNA expression derived significantly greater benefit from treatments like bevacizumab (an anti-VEGF antibody) or regorafenib (a VEGFR/c-Met inhibitor). In two clinical trial cohorts, the high-AIMP2 subgroup showed marked improvement in survival on anti-angiogenic therapy (e.g. in one trial, median survival was substantially longer, with a hazard ratio ~4.75 favoring high AIMP2 patients) (pmc.ncbi.nlm.nih.gov). By contrast, low-AIMP2 tumors did not respond as well to these therapies. The study further identified specific CpG methylation sites in the AIMP2 gene whose methylation status correlated with AIMP2 expression and treatment outcomes (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). For example, hypomethylation at a particular AIMP2 promoter CpG (cg04317940) was associated with elevated AIMP2 and better response to bevacizumab, suggesting an epigenetic marker for patient stratification (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Mechanistically, the link between AIMP2 and angiogenesis may stem from AIMP2’s ability to modulate factors like FUBP1 and TRAF2 that influence VEGF signaling pathways (pmc.ncbi.nlm.nih.gov). In any case, these findings provide “proof-of-concept” that AIMP2 levels can inform therapy decisions. It is an example of translating the functional knowledge of AIMP2 into a practical clinical test: measuring AIMP2 (and AIMP2-DX2) expression or methylation in tumors could help predict which patients will benefit from certain treatments (such as anti-vascular therapies in GBM) (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). This concept may extend to other cancers; as noted earlier, low AIMP2 or high DX2 often signifies a more malignant phenotype, so therapies that either compensate for lost AIMP2 (e.g. via TGF-β induction or pharmacologic stabilization of p53) or specifically target DX2-harboring cells are of high interest.

Expert Perspectives: AIMP2 exemplifies how a classical “housekeeping” protein has evolved additional “moonlighting” functions in higher eukaryotes (pmc.ncbi.nlm.nih.gov). Originally characterized as part of the translation machinery, it is now clear that AIMP2 doubles as a sensor and mediator in multiple signaling pathways that maintain cellular homeostasis. Its ability to shuttle from the cytosolic multisynthetase complex to other cellular compartments (nucleus, membrane complexes, etc.) in response to stress allows it to coordinate the cell’s decision to grow, differentiate, or undergo apoptosis. As a recent review summarized, the three MSC scaffolds (AIMP1, AIMP2, AIMP3) are not merely passive assembly factors – they are “generally considered as auxiliary proteins” that have acquired extra domains/motifs enabling new signaling functions, often acting as tumor suppressors (pmc.ncbi.nlm.nih.gov). In the case of AIMP2, those appended domains (like the GST module) and post-translational modifications (like stress-induced phosphorylation) provide a platform for interacting with various cellular proteins. AIMP2 commonly works by bridging molecules: it brings together a substrate (p53, TRAF2, FBP, or a viral polymerase) with a ubiquitin ligase (MDM2, c-IAP1, Smurf2) or blocks such an interaction, thereby governing the substrate’s stability. This mode of action – serving as an adaptor or competitor in ubiquitin pathways – underlies its suppressive effect on oncogenesis and its pro-apoptotic role in stressed cells (yonsei.elsevierpure.com) (pmc.ncbi.nlm.nih.gov). However, that same pro-apoptotic property necessitates tight regulation, as evidenced by the neurodegenerative impact when AIMP2 is unchecked in Parkinson’s disease models (pmc.ncbi.nlm.nih.gov). Therapeutically, restoring the balance of AIMP2 activity is a key theme: in cancer, augmenting AIMP2 or silencing its antagonist splice form (DX2) is a promising strategy, whereas in neuronal diseases, dampening AIMP2’s toxic interaction with PARP1 has been shown to be beneficial (www.nome.bio) (pmc.ncbi.nlm.nih.gov). Ongoing research in 2023–2024 continues to unveil new facets – from solving the three-dimensional structure of AIMP2-DX2 (to aid drug design) (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov), to exploratory trials of AIMP2-targeted therapies. In summary, AIMP2 is a multifaceted protein that operates at the nexus of protein synthesis and cell signaling. Its primary function is to maintain translational homeostasis in the cytosol, but under the right cues it switches into a regulatory role, safeguarding the organism by triggering apoptosis in damaged or dangerous cells and even defending against viral invasion. This duality makes AIMP2 an intriguing target for medical intervention, as manipulating its levels or interactions could combat diseases ranging from cancer to neurodegeneration. The latest studies and expert analyses highlight AIMP2 as a paradigm of how a core translational factor can be repurposed by the cell to serve as a “guardian” against a variety of threats (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). With its broad influence on critical pathways and a growing recognition in clinical research, AIMP2 is likely to remain an important focus in both fundamental biology and translational medicine in the years to come.

References: Publications and database entries are cited in-line above (with source URLs and identifiers). Key sources include: RefSeq/NCBI Gene summaries (2016), primary research articles by Choi et al. (2009) (pmc.ncbi.nlm.nih.gov), Han et al. (2008) (pmc.ncbi.nlm.nih.gov), Park et al. (2010), Kim et al. (2016) (yonsei.elsevierpure.com), and others, as well as recent reviews in Cell Death & Disease (Zhou et al., 2020) (pmc.ncbi.nlm.nih.gov) and BMB Reports (Kim et al., 2024) (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). These sources, along with the latest studies from 2023–2024 (e.g. Ren et al., 2024 on antiviral function (pmc.ncbi.nlm.nih.gov), and Noor et al., 2023 on glioblastoma biomarkers (pmc.ncbi.nlm.nih.gov)), provide the current understanding of AIMP2’s multifunctional roles and its relevance to human health and disease. The evidence outlined offers a comprehensive view of AIMP2 as both a critical translational scaffold and a versatile signaling hub, reflecting the protein’s evolutionary expansion from a “housekeeper” to a key regulator of cellular fate (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov).

Citations

  1. AnnotationURLCitation(end_index=510, start_index=339, title='AIMP2 aminoacyl tRNA synthetase complex interacting multifunctional protein 2 [Homo sapiens (human)] - Gene - NCBI', type='url_citation', url='https://www.ncbi.nlm.nih.gov/gene?Cmd=DetailsSearch&Term=7965#:~:text=Also%20known%20as%20P38%3B%20JTV1%3B,provided%20by%20RefSeq%2C%20May%202016')
  2. AnnotationURLCitation(end_index=643, start_index=511, title='AIMP2 Gene Disorders: Research Update and Personalized ASO Therapy Options — Nome — Nome', type='url_citation', url='https://www.nome.bio/blog/aimp2-research-aso-therapy#:~:text=AIMP2%20,essential%20for%20two%20cellular%20functions')
  3. AnnotationURLCitation(end_index=1020, start_index=885, title='Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7382500/#:~:text=Aminoacyl,suppressive%20activities.%20In%20addition')
  4. AnnotationURLCitation(end_index=1369, start_index=1199, title='AIMP2 aminoacyl tRNA synthetase complex interacting multifunctional protein 2 [Homo sapiens (human)] - Gene - NCBI', type='url_citation', url='https://www.ncbi.nlm.nih.gov/gene?Cmd=DetailsSearch&Term=7965#:~:text=The%20protein%20encoded%20by%20this,provided%20by%20RefSeq%2C%20May%202016')
  5. AnnotationURLCitation(end_index=1553, start_index=1370, title='- AIMP2 antibodies | Antibodypedia', type='url_citation', url='https://www.antibodypedia.com/gene_details.php?ensembl_id=ENSG00000106305#:~:text=The%20protein%20encoded%20by%20this,provided%20by%20RefSeq%2C%20May%202016')
  6. AnnotationURLCitation(end_index=1874, start_index=1727, title='AIMP2 Gene Disorders: Research Update and Personalized ASO Therapy Options — Nome — Nome', type='url_citation', url='https://www.nome.bio/blog/aimp2-research-aso-therapy#:~:text=activator%20of%20MYC%2C%20thereby%20controlling,cell%20proliferation')
  7. AnnotationURLCitation(end_index=2366, start_index=2237, title='Case Report: Mutation in AIMP2/P38, the Scaffold for the Multi-Trna Synthetase Complex, and Association With Progressive Neurodevelopmental Disorders - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC8820504/#:~:text=al,sequence%20patterns%2C%20which%20are%20the')
  8. AnnotationURLCitation(end_index=2822, start_index=2690, title='Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7382500/#:~:text=aspartyl,AIMP2%20by%20hydrogen%20bonds%20between')
  9. AnnotationURLCitation(end_index=2954, start_index=2823, title='Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7382500/#:~:text=the%20%CE%B17,bound%20to%20AIMP3%2C%20and%20the')
  10. AnnotationURLCitation(end_index=3204, start_index=3072, title='Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7382500/#:~:text=aspartyl,AIMP2%20by%20hydrogen%20bonds%20between')
  11. AnnotationURLCitation(end_index=3422, start_index=3293, title='Case Report: Mutation in AIMP2/P38, the Scaffold for the Multi-Trna Synthetase Complex, and Association With Progressive Neurodevelopmental Disorders - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC8820504/#:~:text=al,sequence%20patterns%2C%20which%20are%20the')
  12. AnnotationURLCitation(end_index=3821, start_index=3638, title='- AIMP2 antibodies | Antibodypedia', type='url_citation', url='https://www.antibodypedia.com/gene_details.php?ensembl_id=ENSG00000106305#:~:text=The%20protein%20encoded%20by%20this,provided%20by%20RefSeq%2C%20May%202016')
  13. AnnotationURLCitation(end_index=3954, start_index=3822, title='Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7382500/#:~:text=aspartyl,AIMP2%20by%20hydrogen%20bonds%20between')
  14. AnnotationURLCitation(end_index=4659, start_index=4522, title='Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7382500/#:~:text=form%20a%20multi,DX2%2C%20and%20AIMP3.%20Also%2C%20we')
  15. AnnotationURLCitation(end_index=4764, start_index=4660, title='Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7382500/#:~:text=AIMP2%20and%20cancer')
  16. AnnotationURLCitation(end_index=5069, start_index=4930, title='Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7382500/#:~:text=apoptosis,mediated%20ubiquitination%20and%20degradation')
  17. AnnotationURLCitation(end_index=5222, start_index=5070, title='Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7382500/#:~:text=discovered%20that%20upon%20TGF,the%20ubiquitination%20of%20FBP%20and')
  18. AnnotationURLCitation(end_index=5634, start_index=5475, title='Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7382500/#:~:text=match%20at%20L376%20apoptosis,mediated%20ubiquitination%20and%20degradation')
  19. AnnotationURLCitation(end_index=5998, start_index=5832, title='Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7382500/#:~:text=tumorigenesis.%20Moreover%2C%20TGF,which%20stimulated%20the%20ubiquitination%20and')
  20. AnnotationURLCitation(end_index=6151, start_index=5999, title='Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7382500/#:~:text=discovered%20that%20upon%20TGF,the%20ubiquitination%20of%20FBP%20and')
  21. AnnotationURLCitation(end_index=6719, start_index=6580, title='Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7382500/#:~:text=apoptosis,mediated%20ubiquitination%20and%20degradation')
  22. AnnotationURLCitation(end_index=7049, start_index=6891, title='AIMP2 restricts EV71 replication by recruiting SMURF2 to promote the degradation of 3D polymerase - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11401463/#:~:text=have%20demonstrated%20that%20AIMP2%20acts,Additionally%2C%20it%20promotes')
  23. AnnotationURLCitation(end_index=7566, start_index=7406, title='Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7382500/#:~:text=It%20is%20reported%20that%20AIMP2,supported%20that%20the%20decreased%20AIMP2')
  24. AnnotationURLCitation(end_index=7734, start_index=7567, title='Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7382500/#:~:text=levels%20in%20heterozygous%20AIMP2%20mice,AIMP2%20enhanced%20the%20sensitivity%20to')
  25. AnnotationURLCitation(end_index=8225, start_index=8065, title='Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7382500/#:~:text=It%20is%20reported%20that%20AIMP2,supported%20that%20the%20decreased%20AIMP2')
  26. AnnotationURLCitation(end_index=8808, start_index=8659, title='Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7382500/#:~:text=of%20p53,Conversely%2C%20exogenous%20supplementation%20of%20AIMP2')
  27. AnnotationURLCitation(end_index=9161, start_index=9002, title='Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7382500/#:~:text=match%20at%20L384%20enhanced%20the,This%20finding%20suggests%20that%20AIMP2')
  28. AnnotationURLCitation(end_index=9576, start_index=9427, title='Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7382500/#:~:text=of%20p53,Conversely%2C%20exogenous%20supplementation%20of%20AIMP2')
  29. AnnotationURLCitation(end_index=9812, start_index=9663, title='Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7382500/#:~:text=of%20p53,Conversely%2C%20exogenous%20supplementation%20of%20AIMP2')
  30. AnnotationURLCitation(end_index=10163, start_index=10004, title='Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7382500/#:~:text=match%20at%20L384%20enhanced%20the,This%20finding%20suggests%20that%20AIMP2')
  31. AnnotationURLCitation(end_index=10636, start_index=10486, title='AIMP2 promotes TNFalpha-dependent apoptosis via ubiquitin-mediated degradation of TRAF2 - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/19584093/#:~:text=degradation%20of%20TRAF2%20,in%20a%20macromolecular%20protein%20complex')
  32. AnnotationURLCitation(end_index=11152, start_index=11018, title='Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7382500/#:~:text=Hemizygous%20deletion%20of%20AIMP2%20increased,Min')
  33. AnnotationURLCitation(end_index=11430, start_index=11296, title='Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7382500/#:~:text=Hemizygous%20deletion%20of%20AIMP2%20increased,Min')
  34. AnnotationURLCitation(end_index=11815, start_index=11681, title='Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7382500/#:~:text=Hemizygous%20deletion%20of%20AIMP2%20increased,Min')
  35. AnnotationURLCitation(end_index=12100, start_index=11966, title='Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7382500/#:~:text=Hemizygous%20deletion%20of%20AIMP2%20increased,Min')
  36. AnnotationURLCitation(end_index=12465, start_index=12331, title='Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7382500/#:~:text=Hemizygous%20deletion%20of%20AIMP2%20increased,Min')
  37. AnnotationURLCitation(end_index=13316, start_index=13104, title='Oncogenic mutation of AIMP2/p38 inhibits its tumor-suppressive interaction with Smurf2 - Yonsei University', type='url_citation', url='https://yonsei.elsevierpure.com/en/publications/oncogenic-mutation-of-aimp2p38-inhibits-its-tumor-suppressive-int#:~:text=responsible%20for%20AIMP2,Smurf2%20and%20suggest%20that%20the')
  38. AnnotationURLCitation(end_index=13469, start_index=13317, title='Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7382500/#:~:text=discovered%20that%20upon%20TGF,the%20ubiquitination%20of%20FBP%20and')
  39. AnnotationURLCitation(end_index=13776, start_index=13583, title='Oncogenic mutation of AIMP2/p38 inhibits its tumor-suppressive interaction with Smurf2 - Yonsei University', type='url_citation', url='https://yonsei.elsevierpure.com/en/publications/oncogenic-mutation-of-aimp2p38-inhibits-its-tumor-suppressive-int#:~:text=c,also%20inhibited%20nuclear%20export%20of')
  40. AnnotationURLCitation(end_index=14401, start_index=14208, title='Oncogenic mutation of AIMP2/p38 inhibits its tumor-suppressive interaction with Smurf2 - Yonsei University', type='url_citation', url='https://yonsei.elsevierpure.com/en/publications/oncogenic-mutation-of-aimp2p38-inhibits-its-tumor-suppressive-int#:~:text=c,also%20inhibited%20nuclear%20export%20of')
  41. AnnotationURLCitation(end_index=14788, start_index=14622, title='Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7382500/#:~:text=tumorigenesis.%20Moreover%2C%20TGF,which%20stimulated%20the%20ubiquitination%20and')
  42. AnnotationURLCitation(end_index=14941, start_index=14789, title='Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7382500/#:~:text=discovered%20that%20upon%20TGF,the%20ubiquitination%20of%20FBP%20and')
  43. AnnotationURLCitation(end_index=15641, start_index=15481, title='Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7382500/#:~:text=It%20is%20reported%20that%20AIMP2,supported%20that%20the%20decreased%20AIMP2')
  44. AnnotationURLCitation(end_index=15809, start_index=15642, title='Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7382500/#:~:text=levels%20in%20heterozygous%20AIMP2%20mice,AIMP2%20enhanced%20the%20sensitivity%20to')
  45. AnnotationURLCitation(end_index=16464, start_index=16323, title='Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7382500/#:~:text=Interestingly%2C%20AIMP2%20was%20a%20Parkin,showed%20that')
  46. AnnotationURLCitation(end_index=16732, start_index=16591, title='Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7382500/#:~:text=Interestingly%2C%20AIMP2%20was%20a%20Parkin,showed%20that')
  47. AnnotationURLCitation(end_index=17302, start_index=17142, title='Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7382500/#:~:text=match%20at%20L188%20AIMP2%20accumulation,to%20delay%20the%20progression%20of')
  48. AnnotationURLCitation(end_index=17472, start_index=17303, title='Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7382500/#:~:text=AIMP2%20accumulation%20overactivated%20poly%28ADP,to%20delay%20the%20progression%20of')
  49. AnnotationURLCitation(end_index=17935, start_index=17794, title='Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7382500/#:~:text=Interestingly%2C%20AIMP2%20was%20a%20Parkin,showed%20that')
  50. AnnotationURLCitation(end_index=18077, start_index=17936, title='Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7382500/#:~:text=associated%20protein%2035%20,USP29%29%2C%20resulting%20in')
  51. AnnotationURLCitation(end_index=18625, start_index=18510, title="Bi-directional regulation of AIMP2 and its splice variant on PARP-1-dependent neuronal cell death; Therapeutic implication for Parkinson's disease - PMC", type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10765824/#:~:text=disease%20,1%20more%20strongly')
  52. AnnotationURLCitation(end_index=18808, start_index=18626, title='AIMP2 Gene Disorders: Research Update and Personalized ASO Therapy Options — Nome — Nome', type='url_citation', url='https://www.nome.bio/blog/aimp2-research-aso-therapy#:~:text=Gene%20therapy%3A%20AAV2%20vectors%20delivering,DX2%20overexpression%20showing%20therapeutic%20efficacy')
  53. AnnotationURLCitation(end_index=19296, start_index=19124, title='AIMP2 Gene Disorders: Research Update and Personalized ASO Therapy Options — Nome — Nome', type='url_citation', url='https://www.nome.bio/blog/aimp2-research-aso-therapy#:~:text=match%20at%20L240%20Gene%20therapy%3A,DX2%20overexpression%20showing%20therapeutic%20efficacy')
  54. AnnotationURLCitation(end_index=19921, start_index=19764, title='AIMP2 restricts EV71 replication by recruiting SMURF2 to promote the degradation of 3D polymerase - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11401463/#:~:text=we%20identified%20a%20novel%20host,the%20antiviral%20effect%20of%20AIMP2')
  55. AnnotationURLCitation(end_index=20072, start_index=19922, title='AIMP2 restricts EV71 replication by recruiting SMURF2 to promote the degradation of 3D polymerase - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11401463/#:~:text=In%20this%20study%2C%20we%20found,Our%20findings%20suggest%20that')
  56. AnnotationURLCitation(end_index=20406, start_index=20249, title='AIMP2 restricts EV71 replication by recruiting SMURF2 to promote the degradation of 3D polymerase - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11401463/#:~:text=we%20identified%20a%20novel%20host,the%20antiviral%20effect%20of%20AIMP2')
  57. AnnotationURLCitation(end_index=20569, start_index=20407, title='AIMP2 restricts EV71 replication by recruiting SMURF2 to promote the degradation of 3D polymerase - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11401463/#:~:text=AIMP2%20recruits%20the%20E3%20ligase,and%20degradation%20of%203D%20polymerase')
  58. AnnotationURLCitation(end_index=20870, start_index=20713, title='AIMP2 restricts EV71 replication by recruiting SMURF2 to promote the degradation of 3D polymerase - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11401463/#:~:text=we%20identified%20a%20novel%20host,the%20antiviral%20effect%20of%20AIMP2')
  59. AnnotationURLCitation(end_index=21033, start_index=20871, title='AIMP2 restricts EV71 replication by recruiting SMURF2 to promote the degradation of 3D polymerase - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11401463/#:~:text=AIMP2%20recruits%20the%20E3%20ligase,and%20degradation%20of%203D%20polymerase')
  60. AnnotationURLCitation(end_index=21342, start_index=21203, title='AIMP2 restricts EV71 replication by recruiting SMURF2 to promote the degradation of 3D polymerase - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11401463/#:~:text=match%20at%20L322%20amounts%20of,qPCR%20analysis%20was')
  61. AnnotationURLCitation(end_index=21493, start_index=21343, title='AIMP2 restricts EV71 replication by recruiting SMURF2 to promote the degradation of 3D polymerase - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11401463/#:~:text=In%20this%20study%2C%20we%20found,Our%20findings%20suggest%20that')
  62. AnnotationURLCitation(end_index=21843, start_index=21693, title='AIMP2 restricts EV71 replication by recruiting SMURF2 to promote the degradation of 3D polymerase - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11401463/#:~:text=In%20this%20study%2C%20we%20found,Our%20findings%20suggest%20that')
  63. AnnotationURLCitation(end_index=22195, start_index=22061, title='AIMP2 restricts EV71 replication by recruiting SMURF2 to promote the degradation of 3D polymerase - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11401463/#:~:text=3,was%20downregulated%20during%20EV71%20infection')
  64. AnnotationURLCitation(end_index=22824, start_index=22634, title='AIMP2 restricts EV71 replication by recruiting SMURF2 to promote the degradation of 3D polymerase - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11401463/#:~:text=regulatory%20function%20of%20AIMP2%20during,development%20of%20antienteroviral%20therapeutic%20strategies')
  65. AnnotationURLCitation(end_index=22975, start_index=22825, title='AIMP2 restricts EV71 replication by recruiting SMURF2 to promote the degradation of 3D polymerase - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11401463/#:~:text=In%20this%20study%2C%20we%20found,Our%20findings%20suggest%20that')
  66. AnnotationURLCitation(end_index=23616, start_index=23474, title='Identification and structure of AIMP2-DX2 for therapeutic perspectives - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11289502/#:~:text=tumorigenesis%20%282,suppressive%20activity%20of%20native')
  67. AnnotationURLCitation(end_index=23774, start_index=23617, title='AIMP2 restricts EV71 replication by recruiting SMURF2 to promote the degradation of 3D polymerase - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11401463/#:~:text=we%20identified%20a%20novel%20host,the%20antiviral%20effect%20of%20AIMP2')
  68. AnnotationURLCitation(end_index=24359, start_index=24195, title='AIMP2 aminoacyl tRNA synthetase complex interacting multifunctional protein 2 [Homo sapiens (human)] - Gene - NCBI', type='url_citation', url='https://www.ncbi.nlm.nih.gov/gene?Cmd=DetailsSearch&Term=7965#:~:text=Also%20known%20as%20P38%3B%20JTV1%3B,provided%20by%20RefSeq%2C%20May')
  69. AnnotationURLCitation(end_index=24831, start_index=24672, title='Case Report: Mutation in AIMP2/P38, the Scaffold for the Multi-Trna Synthetase Complex, and Association With Progressive Neurodevelopmental Disorders - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC8820504/#:~:text=variant%20%28c.105C%20,Iranian%20infant%20with%20progressive%20neurological')
  70. AnnotationURLCitation(end_index=24933, start_index=24832, title='Case Report: Mutation in AIMP2/P38, the Scaffold for the Multi-Trna Synthetase Complex, and Association With Progressive Neurodevelopmental Disorders - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC8820504/#:~:text=in%20AIMP2%20,MRI')
  71. AnnotationURLCitation(end_index=25391, start_index=25230, title='Case Report: Mutation in AIMP2/P38, the Scaffold for the Multi-Trna Synthetase Complex, and Association With Progressive Neurodevelopmental Disorders - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC8820504/#:~:text=homozygous%20state%20in%20exon%203,was%20confirmed%20by%20target%20sequencing')
  72. AnnotationURLCitation(end_index=25551, start_index=25392, title='Case Report: Mutation in AIMP2/P38, the Scaffold for the Multi-Trna Synthetase Complex, and Association With Progressive Neurodevelopmental Disorders - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC8820504/#:~:text=variant%20%28c.105C%20,Iranian%20infant%20with%20progressive%20neurological')
  73. AnnotationURLCitation(end_index=26173, start_index=26026, title='AIMP2 Gene Disorders: Research Update and Personalized ASO Therapy Options — Nome — Nome', type='url_citation', url='https://www.nome.bio/blog/aimp2-research-aso-therapy#:~:text=activator%20of%20MYC%2C%20thereby%20controlling,cell%20proliferation')
  74. AnnotationURLCitation(end_index=26536, start_index=26378, title='Case Report: Mutation in AIMP2/P38, the Scaffold for the Multi-Trna Synthetase Complex, and Association With Progressive Neurodevelopmental Disorders - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC8820504/#:~:text=match%20at%20L47%20AIMP2%20mutation,well%20as%20for%20disease%20management')
  75. AnnotationURLCitation(end_index=26906, start_index=26774, title='AIMP2 Gene Disorders: Research Update and Personalized ASO Therapy Options — Nome — Nome', type='url_citation', url='https://www.nome.bio/blog/aimp2-research-aso-therapy#:~:text=match%20at%20L275%20ASOs%20targeting,length%20protein')
  76. AnnotationURLCitation(end_index=27057, start_index=26907, title='AIMP2 Gene Disorders: Research Update and Personalized ASO Therapy Options — Nome — Nome', type='url_citation', url='https://www.nome.bio/blog/aimp2-research-aso-therapy#:~:text=match%20at%20L372%20%2A%20AIMP2,ASOs%20promoting%20exon%202%20inclusion')
  77. AnnotationURLCitation(end_index=27647, start_index=27494, title='Identification and structure of AIMP2-DX2 for therapeutic perspectives - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11289502/#:~:text=AIMP2%20is%20a%2035%20kDa,produce%20a%20splicing%20variant%20lacking')
  78. AnnotationURLCitation(end_index=27778, start_index=27648, title='Identification and structure of AIMP2-DX2 for therapeutic perspectives - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11289502/#:~:text=exon%202%2C%20known%20as%20AIMP2,Additionally')
  79. AnnotationURLCitation(end_index=28101, start_index=27959, title='Identification and structure of AIMP2-DX2 for therapeutic perspectives - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11289502/#:~:text=tumorigenesis%20%282,suppressive%20activity%20of%20native')
  80. AnnotationURLCitation(end_index=28255, start_index=28102, title='Identification and structure of AIMP2-DX2 for therapeutic perspectives - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11289502/#:~:text=AIMP2%20is%20a%2035%20kDa,produce%20a%20splicing%20variant%20lacking')
  81. AnnotationURLCitation(end_index=28671, start_index=28520, title='Identification and structure of AIMP2-DX2 for therapeutic perspectives - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11289502/#:~:text=competitive%20interactions%20with%20FBP%2C%20TRAF2%2C,2B%29%20%285')
  82. AnnotationURLCitation(end_index=29183, start_index=29019, title='Identification and structure of AIMP2-DX2 for therapeutic perspectives - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11289502/#:~:text=with%20the%20aggressiveness%20of%20certain,suppressive%20activity%20of%20native')
  83. AnnotationURLCitation(end_index=29335, start_index=29184, title='Identification and structure of AIMP2-DX2 for therapeutic perspectives - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11289502/#:~:text=competitive%20interactions%20with%20FBP%2C%20TRAF2%2C,2B%29%20%285')
  84. AnnotationURLCitation(end_index=29666, start_index=29515, title='Identification and structure of AIMP2-DX2 for therapeutic perspectives - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11289502/#:~:text=competitive%20interactions%20with%20FBP%2C%20TRAF2%2C,2B%29%20%285')
  85. AnnotationURLCitation(end_index=30161, start_index=29989, title='AIMP2 Gene Disorders: Research Update and Personalized ASO Therapy Options — Nome — Nome', type='url_citation', url='https://www.nome.bio/blog/aimp2-research-aso-therapy#:~:text=competitively%20inhibiting%20AIMP2%20tumor,associated%20with%20decreased%20overall%20survival')
  86. AnnotationURLCitation(end_index=30558, start_index=30420, title='Identification and structure of AIMP2-DX2 for therapeutic perspectives - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11289502/#:~:text=AIMP2,therapeutic%20strategy%20for%20cancer%20control')
  87. AnnotationURLCitation(end_index=31007, start_index=30875, title='AIMP2 Gene Disorders: Research Update and Personalized ASO Therapy Options — Nome — Nome', type='url_citation', url='https://www.nome.bio/blog/aimp2-research-aso-therapy#:~:text=match%20at%20L275%20ASOs%20targeting,length%20protein')
  88. AnnotationURLCitation(end_index=31128, start_index=31008, title='AIMP2 Gene Disorders: Research Update and Personalized ASO Therapy Options — Nome — Nome', type='url_citation', url='https://www.nome.bio/blog/aimp2-research-aso-therapy#:~:text=ASOs%20targeting%20AIMP2,length%20protein')
  89. AnnotationURLCitation(end_index=31566, start_index=31420, title='AIMP2 Gene Disorders: Research Update and Personalized ASO Therapy Options — Nome — Nome', type='url_citation', url='https://www.nome.bio/blog/aimp2-research-aso-therapy#:~:text=Multiple%20compounds%20targeting%20AIMP2,to%20preclinical%20testing')
  90. AnnotationURLCitation(end_index=31926, start_index=31789, title='AIMP2 Gene Disorders: Research Update and Personalized ASO Therapy Options — Nome — Nome', type='url_citation', url='https://www.nome.bio/blog/aimp2-research-aso-therapy#:~:text=match%20at%20L254%20%2A%20BC,dependent%20tumor%20reduction')
  91. AnnotationURLCitation(end_index=32044, start_index=31927, title='AIMP2 Gene Disorders: Research Update and Personalized ASO Therapy Options — Nome — Nome', type='url_citation', url='https://www.nome.bio/blog/aimp2-research-aso-therapy#:~:text=%2A%20BC,dependent%20tumor%20reduction')
  92. AnnotationURLCitation(end_index=32791, start_index=32620, title='Response to Antiangiogenic Therapy Is Associated with AIMP Protein Family Expression in Glioblastoma and Lower-Grade Gliomas - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC12438089/#:~:text=antiangiogenic%20drugs%2C%20we%20found%20that,cell%20analysis%20revealed%20homogeneous')
  93. AnnotationURLCitation(end_index=32954, start_index=32792, title='Response to Antiangiogenic Therapy Is Associated with AIMP Protein Family Expression in Glioblastoma and Lower-Grade Gliomas - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC12438089/#:~:text=match%20at%20L51%20This%20study,methylation%20status%20offer%20a%20clinically')
  94. AnnotationURLCitation(end_index=33576, start_index=33405, title='Response to Antiangiogenic Therapy Is Associated with AIMP Protein Family Expression in Glioblastoma and Lower-Grade Gliomas - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC12438089/#:~:text=antiangiogenic%20drugs%2C%20we%20found%20that,cell%20analysis%20revealed%20homogeneous')
  95. AnnotationURLCitation(end_index=33984, start_index=33813, title='Response to Antiangiogenic Therapy Is Associated with AIMP Protein Family Expression in Glioblastoma and Lower-Grade Gliomas - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC12438089/#:~:text=antiangiogenic%20drugs%2C%20we%20found%20that,cell%20analysis%20revealed%20homogeneous')
  96. AnnotationURLCitation(end_index=34167, start_index=33985, title='Response to Antiangiogenic Therapy Is Associated with AIMP Protein Family Expression in Glioblastoma and Lower-Grade Gliomas - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC12438089/#:~:text=%281.17%E2%80%934.49%29%2C%20P%20%3D%200.015%5D.%20AIMP2,cell%20analysis%20revealed%20homogeneous')
  97. AnnotationURLCitation(end_index=34547, start_index=34376, title='Response to Antiangiogenic Therapy Is Associated with AIMP Protein Family Expression in Glioblastoma and Lower-Grade Gliomas - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC12438089/#:~:text=antiangiogenic%20drugs%2C%20we%20found%20that,cell%20analysis%20revealed%20homogeneous')
  98. AnnotationURLCitation(end_index=34730, start_index=34548, title='Response to Antiangiogenic Therapy Is Associated with AIMP Protein Family Expression in Glioblastoma and Lower-Grade Gliomas - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC12438089/#:~:text=%281.17%E2%80%934.49%29%2C%20P%20%3D%200.015%5D.%20AIMP2,cell%20analysis%20revealed%20homogeneous')
  99. AnnotationURLCitation(end_index=35035, start_index=34899, title='Response to Antiangiogenic Therapy Is Associated with AIMP Protein Family Expression in Glioblastoma and Lower-Grade Gliomas - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC12438089/#:~:text=match%20at%20L99%20,33%2C%2034%29%20that%20modulate')
  100. AnnotationURLCitation(end_index=35591, start_index=35422, title='Response to Antiangiogenic Therapy Is Associated with AIMP Protein Family Expression in Glioblastoma and Lower-Grade Gliomas - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC12438089/#:~:text=This%20study%20identifies%20AIMP2%20as,methylation%20status%20offer%20a%20clinically')
  101. AnnotationURLCitation(end_index=35783, start_index=35592, title='Response to Antiangiogenic Therapy Is Associated with AIMP Protein Family Expression in Glioblastoma and Lower-Grade Gliomas - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC12438089/#:~:text=groups%20indicate%20that%20AIMPs%2C%20particularly,antiangiogenic%20monotherapy%20was%20more%20efficacious')
  102. AnnotationURLCitation(end_index=36371, start_index=36250, title='Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7382500/#:~:text=Aminoacyl,as%20a%20cleavage%20product')
  103. AnnotationURLCitation(end_index=37256, start_index=37093, title='Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7382500/#:~:text=systems%2C%20eight%20ARSs%20and%20three,this%20review%2C%20we%20summarize%20the')
  104. AnnotationURLCitation(end_index=38078, start_index=37885, title='Oncogenic mutation of AIMP2/p38 inhibits its tumor-suppressive interaction with Smurf2 - Yonsei University', type='url_citation', url='https://yonsei.elsevierpure.com/en/publications/oncogenic-mutation-of-aimp2p38-inhibits-its-tumor-suppressive-int#:~:text=c,also%20inhibited%20nuclear%20export%20of')
  105. AnnotationURLCitation(end_index=38238, start_index=38079, title='Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7382500/#:~:text=match%20at%20L384%20enhanced%20the,This%20finding%20suggests%20that%20AIMP2')
  106. AnnotationURLCitation(end_index=38534, start_index=38412, title='Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7382500/#:~:text=degradation%20of%20AIMP2,showed%20that')
  107. AnnotationURLCitation(end_index=39003, start_index=38821, title='AIMP2 Gene Disorders: Research Update and Personalized ASO Therapy Options — Nome — Nome', type='url_citation', url='https://www.nome.bio/blog/aimp2-research-aso-therapy#:~:text=Gene%20therapy%3A%20AAV2%20vectors%20delivering,DX2%20overexpression%20showing%20therapeutic%20efficacy')
  108. AnnotationURLCitation(end_index=39119, start_index=39004, title="Bi-directional regulation of AIMP2 and its splice variant on PARP-1-dependent neuronal cell death; Therapeutic implication for Parkinson's disease - PMC", type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10765824/#:~:text=disease%20,1%20more%20strongly')
  109. AnnotationURLCitation(end_index=39416, start_index=39263, title='Identification and structure of AIMP2-DX2 for therapeutic perspectives - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11289502/#:~:text=AIMP2%20is%20a%2035%20kDa,produce%20a%20splicing%20variant%20lacking')
  110. AnnotationURLCitation(end_index=39547, start_index=39417, title='Identification and structure of AIMP2-DX2 for therapeutic perspectives - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11289502/#:~:text=exon%202%2C%20known%20as%20AIMP2,Additionally')
  111. AnnotationURLCitation(end_index=40482, start_index=40345, title='Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7382500/#:~:text=form%20a%20multi,DX2%2C%20and%20AIMP3.%20Also%2C%20we')
  112. AnnotationURLCitation(end_index=40587, start_index=40483, title='Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7382500/#:~:text=AIMP2%20and%20cancer')
  113. AnnotationURLCitation(end_index=41172, start_index=41023, title='Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7382500/#:~:text=of%20p53,Conversely%2C%20exogenous%20supplementation%20of%20AIMP2')
  114. AnnotationURLCitation(end_index=41352, start_index=41194, title='AIMP2 restricts EV71 replication by recruiting SMURF2 to promote the degradation of 3D polymerase - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11401463/#:~:text=have%20demonstrated%20that%20AIMP2%20acts,Additionally%2C%20it%20promotes')
  115. AnnotationURLCitation(end_index=41589, start_index=41396, title='Oncogenic mutation of AIMP2/p38 inhibits its tumor-suppressive interaction with Smurf2 - Yonsei University', type='url_citation', url='https://yonsei.elsevierpure.com/en/publications/oncogenic-mutation-of-aimp2p38-inhibits-its-tumor-suppressive-int#:~:text=c,also%20inhibited%20nuclear%20export%20of')
  116. AnnotationURLCitation(end_index=41837, start_index=41677, title='Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7382500/#:~:text=It%20is%20reported%20that%20AIMP2,supported%20that%20the%20decreased%20AIMP2')
  117. AnnotationURLCitation(end_index=42019, start_index=41877, title='Identification and structure of AIMP2-DX2 for therapeutic perspectives - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11289502/#:~:text=tumorigenesis%20%282,suppressive%20activity%20of%20native')
  118. AnnotationURLCitation(end_index=42171, start_index=42020, title='Identification and structure of AIMP2-DX2 for therapeutic perspectives - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11289502/#:~:text=competitive%20interactions%20with%20FBP%2C%20TRAF2%2C,2B%29%20%285')
  119. AnnotationURLCitation(end_index=42437, start_index=42280, title='AIMP2 restricts EV71 replication by recruiting SMURF2 to promote the degradation of 3D polymerase - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11401463/#:~:text=we%20identified%20a%20novel%20host,the%20antiviral%20effect%20of%20AIMP2')
  120. AnnotationURLCitation(end_index=42661, start_index=42490, title='Response to Antiangiogenic Therapy Is Associated with AIMP Protein Family Expression in Glioblastoma and Lower-Grade Gliomas - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC12438089/#:~:text=antiangiogenic%20drugs%2C%20we%20found%20that,cell%20analysis%20revealed%20homogeneous')
  121. AnnotationURLCitation(end_index=43152, start_index=43015, title='Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7382500/#:~:text=form%20a%20multi,DX2%2C%20and%20AIMP3.%20Also%2C%20we')
  122. AnnotationURLCitation(end_index=43257, start_index=43153, title='Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7382500/#:~:text=AIMP2%20and%20cancer')