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BCAT1 Associates with DNA Repair Proteins KU70 and KU80 and Contributes to Regulate DNA Repair in T-Cell Acute Lymphoblastic Leukemia (T-ALL)
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作者:

Tosello, Valeria
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Veneto Inst Oncol IOV, Basic & Translat Oncol Unit, IRCCS, I-35127 Padua, Italy Veneto Inst Oncol IOV, Basic & Translat Oncol Unit, IRCCS, I-35127 Padua, Italy

Rompietti, Chiara
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Veneto Inst Oncol IOV, Immunol & Mol Oncol Diagnost, IRCCS, I-35128 Padua, Italy Veneto Inst Oncol IOV, Basic & Translat Oncol Unit, IRCCS, I-35127 Padua, Italy

Papathanassiu, Adonia E.
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Ergon Pharmaceut LLC, Washington, DC 20011 USA Veneto Inst Oncol IOV, Basic & Translat Oncol Unit, IRCCS, I-35127 Padua, Italy

Arrigoni, Giorgio
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机构:
Univ Padua, Dept Biomed Sci, I-35122 Padua, Italy
Univ Padua, Prote Ctr, I-35131 Padua, Italy
Azienda Osped Padua, I-35131 Padua, Italy Veneto Inst Oncol IOV, Basic & Translat Oncol Unit, IRCCS, I-35127 Padua, Italy

Piovan, Erich
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Veneto Inst Oncol IOV, Immunol & Mol Oncol Diagnost, IRCCS, I-35128 Padua, Italy
Univ Padua, Dept Surg Oncol & Gastroenterol, I-35128 Padua, Italy Veneto Inst Oncol IOV, Basic & Translat Oncol Unit, IRCCS, I-35127 Padua, Italy
机构:
[1] Veneto Inst Oncol IOV, Basic & Translat Oncol Unit, IRCCS, I-35127 Padua, Italy
[2] Veneto Inst Oncol IOV, Immunol & Mol Oncol Diagnost, IRCCS, I-35128 Padua, Italy
[3] Ergon Pharmaceut LLC, Washington, DC 20011 USA
[4] Univ Padua, Dept Biomed Sci, I-35122 Padua, Italy
[5] Univ Padua, Prote Ctr, I-35131 Padua, Italy
[6] Azienda Osped Padua, I-35131 Padua, Italy
[7] Univ Padua, Dept Surg Oncol & Gastroenterol, I-35128 Padua, Italy
关键词:
T-cell lymphoblastic leukemia;
metabolism;
BCAT1;
leukemia growth;
C-MYC;
NOTCH1;
DAMAGE;
ACETYLATION;
ACTIVATION;
D O I:
10.3390/ijms252413571
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
摘要:
Increased expression of branched-chain amino acid (BCAA) transaminase 1 (BCAT1) often correlates with tumor aggressiveness and drug resistance in cancer. We have recently reported that BCAT1 was overexpressed in a subgroup of T-cell acute lymphoblastic (T-ALL) samples, especially those with NOTCH1 activating mutations. Interestingly, BCAT1-depleted cells showed pronounced sensitivity to DNA-damaging agents such as etoposide; however, how BCAT1 regulates this sensitivity remains uncertain. Here, we provide further clues on its chemo-sensitizing effect. Indeed, BCAT1 protein regulates the non-homologous end joining (c-NHEJ) DNA repair pathway by physically associating with the KU70/KU80 heterodimer. BCAT1 inhibition during active repair of DNA double-strand breaks (DSBs) led to increased KU70/KU80 acetylation and impaired c-NHEJ repair, a dramatic increase in DSBs, and ultimately cell death. Our results suggest that, in T-ALL, BCAT1 possesses non-metabolic functions that confer a drug resistance mechanism and that targeting BCAT1 activity presents a novel strategy to improve chemotherapy response in T-ALL patients.
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