Genomic structure and chromosomal localization of the gene encoding TRAX, a Translin-associated factor X

Meng, Guowang; Aoki, Katsunori; Tokura, Katsunobu; Nakahara, Kazuhiko; Inazawa, Johji; Kasai, Masataka

doi:10.1007/s100380070022

Cited by 7 publications

(6 citation statements)

References 9 publications

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“…One clone product gave specific activation with the translin bait. Its nucleotide sequence revealed an open reading frame encoding a protein of 290 amino acids with a predicted molecular weight of 33 kDa, and the encoded protein was named TRAX . TRAX exhibits extensive amino acid homology with translin.…”

Section: Identification and Characterization Of Traxmentioning

confidence: 99%

Mesenchymal cell differentiation and diseases: involvement of translin/TRAX complexes and associated proteins

Kasai

Ishida

Nakahara

et al. 2018

Annals of the New York Academy of Sciences

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Translin and translin-associated factor X (translin/TRAX) proteins have been implicated in a variety of cellular activities central to nucleic acid metabolism. Accumulating evidence indicates that translin/TRAX complexes participate in processes ensuring the replication of DNA, as well as cell division. Significant progress has been made in understanding the roles of translin/TRAX complexes in RNA metabolism, such as through RNA-induced silencing complex activation or the microRNA depletion that occurs in Dicer deficiency. At the cellular level, translin-deficient (Tsn ) mice display delayed endochondral ossification or progressive bone marrow failure with ectopic osteogenesis and adipogenesis, suggesting involvement in mesenchymal cell differentiation. In this review, we summarize the molecular and cellular functions of translin homo-octamer and translin/TRAX hetero-octamer. Finally, we discuss the multifaceted roles of translin, TRAX, and associated proteins in the healthy and disease states.

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Section: Identification and Characterization Of Traxmentioning

confidence: 99%

Mesenchymal cell differentiation and diseases: involvement of translin/TRAX complexes and associated proteins

Kasai

Ishida

Nakahara

et al. 2018

Annals of the New York Academy of Sciences

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“…To identify the location at which TRAX exerts its protective effect, we created a TRAX mutant that lacks the nuclear localization signal (NLS; amino acids [11][12][13][14][15][16][17][18][19][20][21][22][23][24][25][26][27] and is fused to a V5-tag (designated ΔNLS-V5). As shown in Figure 3d, ΔNLS-V5 was located mainly in the cytoplasmic region.…”

Section: Development Of a Trax-null Mouse Model Using The Gene-trap Mmentioning

confidence: 99%

“…18 TRAX and Translin share extensive amino acid homology and form heterodimers to mediate biological functions, including chromosomal translocations, genome stability regulation, dendritic trafficking of brain-derived neurotrophic factor mRNA, spermatogenesis and neuronal development. [19][20][21][22] Independent to Translin, TRAX alone regulates axonal regeneration 23 and rescuing impaired neuronal differentiation caused by p53 blockade. 24,25 In response to DNA damage, TRAX interacts directly with C1D, a nuclear matrix protein participating in DNA repair.…”

Section: Introductionmentioning

confidence: 99%

A central role of TRAX in the ATM-mediated DNA repair

et al. 2015

Oncogene

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DNA repair is critical for the maintenance of genome stability. Upon genotoxic stress, dysregulated DNA repair may induce apoptosis. Translin-associated factor X (TRAX), which was initially identified as a binding partner of Translin, has been implicated in genome stability. However, the exact role of TRAX in DNA repair remains largely unknown. Here, we showed that TRAX participates in the ATM/H2AX-mediated DNA repair machinery by interacting with ATM and stabilizing the MRN complex at double-strand breaks. The exogenous expression of wild-type (WT) TRAX, but not a TRAX variant lacking the nuclear localization signal (NLS), rescued the vulnerability of TRAX-null mouse embryo fibroblasts (MEFs). This finding confirms the importance of the nuclear localization of TRAX in the repair of DNA damage. Compared with WT MEFs, TRAX-null MEFs exhibited impaired DNA repair (for example, reduced phosphorylation of ATM and H2AX) after treatment with ultra violet-C or γ-ray irradiation and a higher incidence of p53-mediated apoptosis. Our findings demonstrate that TRAX is required for MRN complex-ATM-H2AX signaling, which optimizes DNA repair by interacting with the activated ATM and protects cells from genotoxic stress-induced apoptosis.

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“…Using inhibitors of PKA or GSK3beta to test the role of these signaling pathways in mediating dissociation of trax from A 2A R, they found that: 1) inhibition of PKA blocks the ability of A 2A R stimulation to phosphorylate GSK3β, and 2) GSK3β inhibition triggers dissociation of trax from the A 2A R. Further examination of the interaction between GSK3β and trax revealed that they co-precipitate along with Disrupted-in-Schizophrenia 1 (DISCI), a protein known to interact with GSK3P [5]{Chien, 2018 #6}. Detection of a physical interaction between DISCI and trax is of particular interest because these two proteins are encoded by two genes (namely DISCI and TSNAX) that are located adjacent to each other on human chromosome 1 in a region that has been implicated in major mental disorders (such as schizophrenia, autism, depression, and bipolar disorder) [29][30][31][32][33][34].…”

Section: Role Of Trax In the Nucleus: Dna Repairmentioning

confidence: 99%

Trax: A versatile signaling protein plays key roles in synaptic plasticity and DNA repair

Chern

Chien

et al. 2019

Neurobiology of Learning and Memory

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Translin-associated protein X (TSNAX), also called trax, was first identified as a protein that interacts with translin. Subsequent studies demonstrated that these proteins form a heteromeric RNase complex that mediates degradation of microRNAs, a pivotal finding that has stimulated interest in understanding the role of translin and trax in cell signaling. Recent studies addressing this question have revealed that trax plays key roles in both synaptic plasticity and DNA repair signaling pathways. In the context of synaptic plasticity, trax works together with its partner protein, translin, to degrade a subset of microRNAs. Activation of the translin/trax RNase complex reverses microRNA-mediated translational silencing to trigger dendritic protein synthesis critical for synaptic plasticity. In the context of DNA repair, trax binds to and activates ATM, a central component of the double-stranded DNA repair process. Thus, these studies focus attention on trax as a critical signaling protein that interacts with multiple partners to impact diverse signaling pathways. To stimulate interest in deciphering the multifaceted role of trax in cell signaling, we summarize the current understanding of trax biology and highlight gaps in our knowledge about this protean protein.

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Genomic structure and chromosomal localization of the gene encoding TRAX, a Translin-associated factor X

Cited by 7 publications

References 9 publications

Mesenchymal cell differentiation and diseases: involvement of translin/TRAX complexes and associated proteins

Mesenchymal cell differentiation and diseases: involvement of translin/TRAX complexes and associated proteins

A central role of TRAX in the ATM-mediated DNA repair

Trax: A versatile signaling protein plays key roles in synaptic plasticity and DNA repair

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