Cellular processing determinants for the activation of damage signals in response to topoisomerase I-linked DNA breakage

TY - JOUR

T1 - Cellular processing determinants for the activation of damage signals in response to topoisomerase I-linked DNA breakage

AU - Huang, Ting-Hsiang

AU - Chen, Hsiang-Chin

AU - Chou, Shang-Min

AU - Yang, Yu-Chen

AU - Fan, Jia-Rong

AU - Li, Tsai-Kun

N1 - 被引用次數：8 Export Date: 7 April 2016 通訊地址: Li, T.-K.; Department and Graduate Institute of Microbiology, College of Medicine, National Taiwan University, Jen-Ai Road, Taipei 10018, Taiwan; 電子郵件： tsaikunli@ntu.edu.tw 化學物質/CAS: DNA topoisomerase, 80449-01-0; camptothecin, 7689-03-4; checkpoint kinase 2, 244634-79-5; Camptothecin, 7689-03-4; Cell Cycle Proteins; DNA Topoisomerases, Type I, 5.99.1.2; DNA-Binding Proteins; Protein-Serine-Threonine Kinases, 2.7.11.1; RPA2 protein, human, 2.7.7.7; Replication Protein A; Tumor Suppressor Protein p53; Tumor Suppressor Proteins; ataxia telangiectasia mutated protein, 2.7.1.37; checkpoint kinase 2, 2.7.1.37 參考文獻: Zhou, B.B., Bartek, J., Targeting the checkpoint kinases: Chemo-sensitization versus chemoprotection (2004) Nat Rev Cancer, 4, pp. 216-225; Falck, J., Coates, J., Jackson, S.P., Conserved modes of recruitment of ATM. 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PY - 2010

Y1 - 2010

N2 - Recent studies have suggested an involvement of processing pathways for the initiation of cellular responses induced by topoisomerase-targeting drugs. Here, we showed that cellular exposure to camptothecin (CPT) induced formation of topoisomerase I cleavable complex (TOP1cc), degradation of TOP1 and activation of DNA damage responses (DDR). Transcription and proteasome-dependent proteolysis, but not replication, were involved in CPT-induced TOP1 degradation, while none of above three processing activities affected TOP1cc formation. Replication-and transcription-initiated processing (RIP and TIP) of TOP1cc were identified as two independent pathways, which contribute distinctly to various CPT-activated DDR. Specifically, in cycling cells, RIP-processed TOP1cc triggered the CPT-induced RPA phosphorylation. At higher CPT dosages, the TIP pathway is required for other DDR activation, including ATM, p53 and Chk1/2 phosphorylation. The TIP pathway was further demonstrated to be S-phase independent by using three nonreplicating cell models. Furthermore, the effect of proteasome inhibitors mimicked that of transcription inhibition on the CPT-induced activation of DDR, suggesting the involvement of proteasome in the TIP pathway. Interestingly, the TIP pathway was important for TOP1cc-activated, but not ionization radiation-activated ATM, p53 and Chk2 phosphorylation. We have also found that pharmacological interferences of TIP and RIP pathways distinctively modulated the CPT-induced cell killing with treatments at low and high dosages, respectively. Together, our results support that both RIP and TIP pathways of TOP1cc are required for the activation of CPT-induced DDR and cytotoxicity. © 2010 IBCB, SIBS, CAS. All rights reserved.

AB - Recent studies have suggested an involvement of processing pathways for the initiation of cellular responses induced by topoisomerase-targeting drugs. Here, we showed that cellular exposure to camptothecin (CPT) induced formation of topoisomerase I cleavable complex (TOP1cc), degradation of TOP1 and activation of DNA damage responses (DDR). Transcription and proteasome-dependent proteolysis, but not replication, were involved in CPT-induced TOP1 degradation, while none of above three processing activities affected TOP1cc formation. Replication-and transcription-initiated processing (RIP and TIP) of TOP1cc were identified as two independent pathways, which contribute distinctly to various CPT-activated DDR. Specifically, in cycling cells, RIP-processed TOP1cc triggered the CPT-induced RPA phosphorylation. At higher CPT dosages, the TIP pathway is required for other DDR activation, including ATM, p53 and Chk1/2 phosphorylation. The TIP pathway was further demonstrated to be S-phase independent by using three nonreplicating cell models. Furthermore, the effect of proteasome inhibitors mimicked that of transcription inhibition on the CPT-induced activation of DDR, suggesting the involvement of proteasome in the TIP pathway. Interestingly, the TIP pathway was important for TOP1cc-activated, but not ionization radiation-activated ATM, p53 and Chk2 phosphorylation. We have also found that pharmacological interferences of TIP and RIP pathways distinctively modulated the CPT-induced cell killing with treatments at low and high dosages, respectively. Together, our results support that both RIP and TIP pathways of TOP1cc are required for the activation of CPT-induced DDR and cytotoxicity. © 2010 IBCB, SIBS, CAS. All rights reserved.

KW - cleavable complex

KW - DNA damage responses

KW - downregulation

KW - processing

KW - protein-linked DNA break

KW - ATM protein

KW - camptothecin

KW - cell cycle protein

KW - checkpoint kinase 2

KW - DNA binding protein

KW - DNA topoisomerase

KW - protein p53

KW - protein serine threonine kinase

KW - replication factor A

KW - RPA2 protein, human

KW - tumor suppressor protein

KW - article

KW - DNA repair

KW - DNA replication

KW - DNA strand breakage

KW - genetic transcription

KW - genetics

KW - human

KW - metabolism

KW - phosphorylation

KW - signal transduction

KW - tumor cell line

KW - Camptothecin

KW - Cell Cycle Proteins

KW - Cell Line, Tumor

KW - DNA Breaks

KW - DNA Repair

KW - DNA Replication

KW - DNA Topoisomerases, Type I

KW - DNA-Binding Proteins

KW - Humans

KW - Phosphorylation

KW - Protein-Serine-Threonine Kinases

KW - Replication Protein A

KW - Signal Transduction

KW - Transcription, Genetic

KW - Tumor Suppressor Protein p53

KW - Tumor Suppressor Proteins

U2 - 10.1038/cr.2010.95

DO - 10.1038/cr.2010.95

M3 - Article

VL - 20

SP - 1060

EP - 1075

JO - Cell Research

JF - Cell Research

SN - 1001-0602

IS - 9

ER -