On Broken Ne(c)ks and Broken DNA: The Role of Human NEKs in the DNA Damage Response
NIMA-related kinases, or NEKs, are a family of Ser/Thr protein kinases involved in cell cycle and mitosis, centrosome disjunction, primary cilia functions, and DNA damage responses among other biological functional contexts in vertebrate cells. In human cells, there are 11 members, termed NEK1 to 11...
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Published in | Cells (Basel, Switzerland) Vol. 10; no. 3; p. 507 |
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Main Authors | , , , , , , , , , , , |
Format | Journal Article |
Language | English |
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27.02.2021
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Abstract | NIMA-related kinases, or NEKs, are a family of Ser/Thr protein kinases involved in cell cycle and mitosis, centrosome disjunction, primary cilia functions, and DNA damage responses among other biological functional contexts in vertebrate cells. In human cells, there are 11 members, termed NEK1 to 11, and the research has mainly focused on exploring the more predominant roles of NEKs in mitosis regulation and cell cycle. A possible important role of NEKs in DNA damage response (DDR) first emerged for NEK1, but recent studies for most NEKs showed participation in DDR. A detailed analysis of the protein interactions, phosphorylation events, and studies of functional aspects of NEKs from the literature led us to propose a more general role of NEKs in DDR. In this review, we express that NEK1 is an activator of ataxia telangiectasia and Rad3-related (ATR), and its activation results in cell cycle arrest, guaranteeing DNA repair while activating specific repair pathways such as homology repair (HR) and DNA double-strand break (DSB) repair. For NEK2, 6, 8, 9, and 11, we found a role downstream of ATR and ataxia telangiectasia mutated (ATM) that results in cell cycle arrest, but details of possible activated repair pathways are still being investigated. NEK4 shows a connection to the regulation of the nonhomologous end-joining (NHEJ) repair of DNA DSBs, through recruitment of DNA-PK to DNA damage foci. NEK5 interacts with topoisomerase IIβ, and its knockdown results in the accumulation of damaged DNA. NEK7 has a regulatory role in the detection of oxidative damage to telomeric DNA. Finally, NEK10 has recently been shown to phosphorylate p53 at Y327, promoting cell cycle arrest after exposure to DNA damaging agents. In summary, this review highlights important discoveries of the ever-growing involvement of NEK kinases in the DDR pathways. A better understanding of these roles may open new diagnostic possibilities or pharmaceutical interventions regarding the chemo-sensitizing inhibition of NEKs in various forms of cancer and other diseases. |
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AbstractList | NIMA-related kinases, or NEKs, are a family of Ser/Thr protein kinases involved in cell cycle and mitosis, centrosome disjunction, primary cilia functions, and DNA damage responses among other biological functional contexts in vertebrate cells. In human cells, there are 11 members, termed NEK1 to 11, and the research has mainly focused on exploring the more predominant roles of NEKs in mitosis regulation and cell cycle. A possible important role of NEKs in DNA damage response (DDR) first emerged for NEK1, but recent studies for most NEKs showed participation in DDR. A detailed analysis of the protein interactions, phosphorylation events, and studies of functional aspects of NEKs from the literature led us to propose a more general role of NEKs in DDR. In this review, we express that NEK1 is an activator of ataxia telangiectasia and Rad3-related (ATR), and its activation results in cell cycle arrest, guaranteeing DNA repair while activating specific repair pathways such as homology repair (HR) and DNA double-strand break (DSB) repair. For NEK2, 6, 8, 9, and 11, we found a role downstream of ATR and ataxia telangiectasia mutated (ATM) that results in cell cycle arrest, but details of possible activated repair pathways are still being investigated. NEK4 shows a connection to the regulation of the nonhomologous end-joining (NHEJ) repair of DNA DSBs, through recruitment of DNA-PK to DNA damage foci. NEK5 interacts with topoisomerase IIβ, and its knockdown results in the accumulation of damaged DNA. NEK7 has a regulatory role in the detection of oxidative damage to telomeric DNA. Finally, NEK10 has recently been shown to phosphorylate p53 at Y327, promoting cell cycle arrest after exposure to DNA damaging agents. In summary, this review highlights important discoveries of the ever-growing involvement of NEK kinases in the DDR pathways. A better understanding of these roles may open new diagnostic possibilities or pharmaceutical interventions regarding the chemo-sensitizing inhibition of NEKs in various forms of cancer and other diseases. NIMA-related kinases, or NEKs, are a family of Ser/Thr protein kinases involved in cell cycle and mitosis, centrosome disjunction, primary cilia functions, and DNA damage responses among other biological functional contexts in vertebrate cells. In human cells, there are 11 members, termed NEK1 to 11, and the research has mainly focused on exploring the more predominant roles of NEKs in mitosis regulation and cell cycle. A possible important role of NEKs in DNA damage response (DDR) first emerged for NEK1, but recent studies for most NEKs showed participation in DDR. A detailed analysis of the protein interactions, phosphorylation events, and studies of functional aspects of NEKs from the literature led us to propose a more general role of NEKs in DDR. In this review, we express that NEK1 is an activator of ataxia telangiectasia and Rad3-related (ATR), and its activation results in cell cycle arrest, guaranteeing DNA repair while activating specific repair pathways such as homology repair (HR) and DNA double-strand break (DSB) repair. For NEK2, 6, 8, 9, and 11, we found a role downstream of ATR and ataxia telangiectasia mutated (ATM) that results in cell cycle arrest, but details of possible activated repair pathways are still being investigated. NEK4 shows a connection to the regulation of the nonhomologous end-joining (NHEJ) repair of DNA DSBs, through recruitment of DNA-PK to DNA damage foci. NEK5 interacts with topoisomerase IIβ, and its knockdown results in the accumulation of damaged DNA. NEK7 has a regulatory role in the detection of oxidative damage to telomeric DNA. Finally, NEK10 has recently been shown to phosphorylate p53 at Y327, promoting cell cycle arrest after exposure to DNA damaging agents. In summary, this review highlights important discoveries of the ever-growing involvement of NEK kinases in the DDR pathways. A better understanding of these roles may open new diagnostic possibilities or pharmaceutical interventions regarding the chemo-sensitizing inhibition of NEKs in various forms of cancer and other diseases.NIMA-related kinases, or NEKs, are a family of Ser/Thr protein kinases involved in cell cycle and mitosis, centrosome disjunction, primary cilia functions, and DNA damage responses among other biological functional contexts in vertebrate cells. In human cells, there are 11 members, termed NEK1 to 11, and the research has mainly focused on exploring the more predominant roles of NEKs in mitosis regulation and cell cycle. A possible important role of NEKs in DNA damage response (DDR) first emerged for NEK1, but recent studies for most NEKs showed participation in DDR. A detailed analysis of the protein interactions, phosphorylation events, and studies of functional aspects of NEKs from the literature led us to propose a more general role of NEKs in DDR. In this review, we express that NEK1 is an activator of ataxia telangiectasia and Rad3-related (ATR), and its activation results in cell cycle arrest, guaranteeing DNA repair while activating specific repair pathways such as homology repair (HR) and DNA double-strand break (DSB) repair. For NEK2, 6, 8, 9, and 11, we found a role downstream of ATR and ataxia telangiectasia mutated (ATM) that results in cell cycle arrest, but details of possible activated repair pathways are still being investigated. NEK4 shows a connection to the regulation of the nonhomologous end-joining (NHEJ) repair of DNA DSBs, through recruitment of DNA-PK to DNA damage foci. NEK5 interacts with topoisomerase IIβ, and its knockdown results in the accumulation of damaged DNA. NEK7 has a regulatory role in the detection of oxidative damage to telomeric DNA. Finally, NEK10 has recently been shown to phosphorylate p53 at Y327, promoting cell cycle arrest after exposure to DNA damaging agents. In summary, this review highlights important discoveries of the ever-growing involvement of NEK kinases in the DDR pathways. A better understanding of these roles may open new diagnostic possibilities or pharmaceutical interventions regarding the chemo-sensitizing inhibition of NEKs in various forms of cancer and other diseases. |
Author | Simabuco, Fernando Moreira Peres de Oliveira, Andressa Issayama, Luidy Kazuo Basei, Fernanda Luisa Alves Dos Reis Moura, Lívia Rodrigues de Oliveira, Ana Luisa Kobarg, Jörg Dias, Pedro Rafael Firmino Pavan, Isadora Carolina Betim Martins, Mariana Bonjiorno Ferezin, Camila de Castro Silva, Fernando Riback |
AuthorAffiliation | 1 Graduate Program in “Ciências Farmacêuticas”, School of Pharmaceutical Sciences, Faculty of Pharmaceutical Sciences, State University of Campinas (UNICAMP), R. Cândido Portinari 200, Prédio 2, Campinas CEP 13083-871, Brazil; isadora.bpavan@gmail.com (I.C.B.P.); andressa2401@gmail.com (A.P.d.O.); pedrofirminodias@gmail.com (P.R.F.D.); fernandabasei@gmail.com (F.L.B.); kazuo.bio@gmail.com (L.K.I.); fernandoriback@hotmail.com (F.R.S.); aluisa1702@gmail.com (A.L.R.d.O.); l156284@dac.unicamp.br (L.A.d.R.M.); mbonjiorno@gmail.com (M.B.M.) 2 Graduate Program in “Biologia Funcional e Molecular”, Department of Biochemistry and Tissue Biology, Institute of Biology, State University of Campinas (UNICAMP), Campinas 13083-857, Brazil; camilaferezin7@gmail.com 3 School of Applied Sciences, State University of Campinas (UNICAMP), Limeira CEP 13484-350, Brazil; simabuco@gmail.com |
AuthorAffiliation_xml | – name: 1 Graduate Program in “Ciências Farmacêuticas”, School of Pharmaceutical Sciences, Faculty of Pharmaceutical Sciences, State University of Campinas (UNICAMP), R. Cândido Portinari 200, Prédio 2, Campinas CEP 13083-871, Brazil; isadora.bpavan@gmail.com (I.C.B.P.); andressa2401@gmail.com (A.P.d.O.); pedrofirminodias@gmail.com (P.R.F.D.); fernandabasei@gmail.com (F.L.B.); kazuo.bio@gmail.com (L.K.I.); fernandoriback@hotmail.com (F.R.S.); aluisa1702@gmail.com (A.L.R.d.O.); l156284@dac.unicamp.br (L.A.d.R.M.); mbonjiorno@gmail.com (M.B.M.) – name: 2 Graduate Program in “Biologia Funcional e Molecular”, Department of Biochemistry and Tissue Biology, Institute of Biology, State University of Campinas (UNICAMP), Campinas 13083-857, Brazil; camilaferezin7@gmail.com – name: 3 School of Applied Sciences, State University of Campinas (UNICAMP), Limeira CEP 13484-350, Brazil; simabuco@gmail.com |
Author_xml | – sequence: 1 givenname: Isadora Carolina Betim surname: Pavan fullname: Pavan, Isadora Carolina Betim organization: Graduate Program in "Ciências Farmacêuticas", School of Pharmaceutical Sciences, Faculty of Pharmaceutical Sciences, State University of Campinas (UNICAMP), R. Cândido Portinari 200, Prédio 2, Campinas CEP 13083-871, Brazil – sequence: 2 givenname: Andressa surname: Peres de Oliveira fullname: Peres de Oliveira, Andressa organization: Graduate Program in "Ciências Farmacêuticas", School of Pharmaceutical Sciences, Faculty of Pharmaceutical Sciences, State University of Campinas (UNICAMP), R. Cândido Portinari 200, Prédio 2, Campinas CEP 13083-871, Brazil – sequence: 3 givenname: Pedro Rafael Firmino surname: Dias fullname: Dias, Pedro Rafael Firmino organization: Graduate Program in "Ciências Farmacêuticas", School of Pharmaceutical Sciences, Faculty of Pharmaceutical Sciences, State University of Campinas (UNICAMP), R. Cândido Portinari 200, Prédio 2, Campinas CEP 13083-871, Brazil – sequence: 4 givenname: Fernanda Luisa orcidid: 0000-0001-6232-7170 surname: Basei fullname: Basei, Fernanda Luisa organization: Graduate Program in "Ciências Farmacêuticas", School of Pharmaceutical Sciences, Faculty of Pharmaceutical Sciences, State University of Campinas (UNICAMP), R. Cândido Portinari 200, Prédio 2, Campinas CEP 13083-871, Brazil – sequence: 5 givenname: Luidy Kazuo surname: Issayama fullname: Issayama, Luidy Kazuo organization: Graduate Program in "Ciências Farmacêuticas", School of Pharmaceutical Sciences, Faculty of Pharmaceutical Sciences, State University of Campinas (UNICAMP), R. Cândido Portinari 200, Prédio 2, Campinas CEP 13083-871, Brazil – sequence: 6 givenname: Camila de Castro surname: Ferezin fullname: Ferezin, Camila de Castro organization: Graduate Program in "Biologia Funcional e Molecular", Department of Biochemistry and Tissue Biology, Institute of Biology, State University of Campinas (UNICAMP), Campinas 13083-857, Brazil – sequence: 7 givenname: Fernando Riback surname: Silva fullname: Silva, Fernando Riback organization: Graduate Program in "Ciências Farmacêuticas", School of Pharmaceutical Sciences, Faculty of Pharmaceutical Sciences, State University of Campinas (UNICAMP), R. Cândido Portinari 200, Prédio 2, Campinas CEP 13083-871, Brazil – sequence: 8 givenname: Ana Luisa surname: Rodrigues de Oliveira fullname: Rodrigues de Oliveira, Ana Luisa organization: Graduate Program in "Ciências Farmacêuticas", School of Pharmaceutical Sciences, Faculty of Pharmaceutical Sciences, State University of Campinas (UNICAMP), R. Cândido Portinari 200, Prédio 2, Campinas CEP 13083-871, Brazil – sequence: 9 givenname: Lívia surname: Alves Dos Reis Moura fullname: Alves Dos Reis Moura, Lívia organization: Graduate Program in "Ciências Farmacêuticas", School of Pharmaceutical Sciences, Faculty of Pharmaceutical Sciences, State University of Campinas (UNICAMP), R. Cândido Portinari 200, Prédio 2, Campinas CEP 13083-871, Brazil – sequence: 10 givenname: Mariana Bonjiorno orcidid: 0000-0002-9659-6528 surname: Martins fullname: Martins, Mariana Bonjiorno organization: Graduate Program in "Biologia Funcional e Molecular", Department of Biochemistry and Tissue Biology, Institute of Biology, State University of Campinas (UNICAMP), Campinas 13083-857, Brazil – sequence: 11 givenname: Fernando Moreira orcidid: 0000-0002-1672-9686 surname: Simabuco fullname: Simabuco, Fernando Moreira organization: School of Applied Sciences, State University of Campinas (UNICAMP), Limeira CEP 13484-350, Brazil – sequence: 12 givenname: Jörg orcidid: 0000-0002-9419-0145 surname: Kobarg fullname: Kobarg, Jörg organization: Graduate Program in "Biologia Funcional e Molecular", Department of Biochemistry and Tissue Biology, Institute of Biology, State University of Campinas (UNICAMP), Campinas 13083-857, Brazil |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/33673578$$D View this record in MEDLINE/PubMed |
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Keywords | kinase DNA damage response cell cycle protein kinase |
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Snippet | NIMA-related kinases, or NEKs, are a family of Ser/Thr protein kinases involved in cell cycle and mitosis, centrosome disjunction, primary cilia functions, and... |
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SubjectTerms | Apoptosis Ataxia telangiectasia Ataxia telangiectasia mutated protein Cell activation Cell cycle Cell division Chromosomes Cilia Cyclin-dependent kinases Deoxyribonucleic acid DNA DNA damage DNA Damage - genetics DNA damage response DNA repair DNA Repair - genetics DNA-dependent protein kinase Double-strand break repair Gene expression Genomes Homology Humans kinase Kinases Metabolism Mitosis Nek1 protein Non-homologous end joining p53 Protein Phosphorylation Protein interaction protein kinase Proteins Review |
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Title | On Broken Ne(c)ks and Broken DNA: The Role of Human NEKs in the DNA Damage Response |
URI | https://www.ncbi.nlm.nih.gov/pubmed/33673578 https://www.proquest.com/docview/2497030234 https://www.proquest.com/docview/2498486754/abstract/ https://pubmed.ncbi.nlm.nih.gov/PMC7997185 https://doaj.org/article/3656be30a566449698c626134c7f279e |
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