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Lamin A buffers CK2 kinase activity to modulate aging in a progeria mouse model.
Ao, Ying; Zhang, Jie; Liu, Zuojun; Qian, Minxian; Li, Yao; Wu, Zhuping; Sun, Pengfei; Wu, Jie; Bei, Weixin; Wen, Junqu; Wu, Xuli; Li, Feng; Zhou, Zhongjun; Zhu, Wei-Guo; Liu, Baohua; Wang, Zimei.
Affiliation
  • Ao Y; Guangdong Key Laboratory of Genome Stability and Human Disease Prevention, Carson International Cancer Center, Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Health Science Center, Shenzhen 518060, China.
  • Zhang J; Department of Genetics, School of Basic Medical Sciences, Wuhan University, Wuhan 430071, Hubei, China.
  • Liu Z; Guangdong Key Laboratory of Genome Stability and Human Disease Prevention, Carson International Cancer Center, Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Health Science Center, Shenzhen 518060, China.
  • Qian M; Guangdong Key Laboratory of Genome Stability and Human Disease Prevention, Carson International Cancer Center, Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Health Science Center, Shenzhen 518060, China.
  • Li Y; Guangdong Key Laboratory of Genome Stability and Human Disease Prevention, Carson International Cancer Center, Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Health Science Center, Shenzhen 518060, China.
  • Wu Z; School of Public Health, Shenzhen University Health Science Center, Shenzhen 518060, China.
  • Sun P; Guangdong Key Laboratory of Genome Stability and Human Disease Prevention, Carson International Cancer Center, Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Health Science Center, Shenzhen 518060, China.
  • Wu J; Guangdong Key Laboratory of Genome Stability and Human Disease Prevention, Carson International Cancer Center, Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Health Science Center, Shenzhen 518060, China.
  • Bei W; Guangdong Key Laboratory of Genome Stability and Human Disease Prevention, Carson International Cancer Center, Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Health Science Center, Shenzhen 518060, China.
  • Wen J; Guangdong Key Laboratory of Genome Stability and Human Disease Prevention, Carson International Cancer Center, Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Health Science Center, Shenzhen 518060, China.
  • Wu X; Guangdong Key Laboratory of Genome Stability and Human Disease Prevention, Carson International Cancer Center, Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Health Science Center, Shenzhen 518060, China.
  • Li F; School of Public Health, Shenzhen University Health Science Center, Shenzhen 518060, China.
  • Zhou Z; Department of Genetics, School of Basic Medical Sciences, Wuhan University, Wuhan 430071, Hubei, China.
  • Zhu WG; School of Biomedical Sciences, Li Ka Shing Faculty of Medicine, The University of Hong Kong, 21 Sassoon Road, Hong Kong.
  • Liu B; Guangdong Key Laboratory of Genome Stability and Human Disease Prevention, Carson International Cancer Center, Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Health Science Center, Shenzhen 518060, China.
  • Wang Z; Guangdong Key Laboratory of Genome Stability and Human Disease Prevention, Carson International Cancer Center, Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Health Science Center, Shenzhen 518060, China.
Sci Adv ; 5(3): eaav5078, 2019 03.
Article in En | MEDLINE | ID: mdl-30906869
Defective nuclear lamina protein lamin A is associated with premature aging. Casein kinase 2 (CK2) binds the nuclear lamina, and inhibiting CK2 activity induces cellular senescence in cancer cells. Thus, it is feasible that lamin A and CK2 may cooperate in the aging process. Nuclear CK2 localization relies on lamin A and the lamin A carboxyl terminus physically interacts with the CK2α catalytic core and inhibits its kinase activity. Loss of lamin A in Lmna-knockout mouse embryonic fibroblasts (MEFs) confers increased CK2 activity. Conversely, prelamin A that accumulates in Zmpste24-deficent MEFs exhibits a high CK2α binding affinity and concomitantly reduces CK2 kinase activity. Permidine treatment activates CK2 by releasing the interaction between lamin A and CK2, promoting DNA damage repair and ameliorating progeroid features. These data reveal a previously unidentified function for nuclear lamin A and highlight an essential role for CK2 in regulating senescence and aging.
Subject(s)

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Progeria / Aging / Metalloendopeptidases / Lamin Type A / Casein Kinase II / Membrane Proteins Limits: Animals / Humans Language: En Journal: Sci Adv Year: 2019 Document type: Article Affiliation country: China Country of publication: Estados Unidos

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Progeria / Aging / Metalloendopeptidases / Lamin Type A / Casein Kinase II / Membrane Proteins Limits: Animals / Humans Language: En Journal: Sci Adv Year: 2019 Document type: Article Affiliation country: China Country of publication: Estados Unidos