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Article: Lamin A buffers CK2 kinase activity to modulate aging in a progeria mouse model

TitleLamin A buffers CK2 kinase activity to modulate aging in a progeria mouse model
Authors
KeywordsBinding energy
Cell culture
Issue Date2019
PublisherAmerican Association for the Advancement of Science: Science Advances. The Journal's web site is located at http://www.scienceadvances.org/
Citation
Science Advances, 2019, v. 5 n. 3, p. article no. eaav5078 How to Cite?
AbstractDefective 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.
Persistent Identifierhttp://hdl.handle.net/10722/277180
ISSN
2019 Impact Factor: 13.116

 

DC FieldValueLanguage
dc.contributor.authorAo, Y-
dc.contributor.authorZhang, J-
dc.contributor.authorLiu, Z-
dc.contributor.authorQian, M-
dc.contributor.authorLi, Y-
dc.contributor.authorWu, Z-
dc.contributor.authorSun, P-
dc.contributor.authorWu, J-
dc.contributor.authorBei, W-
dc.contributor.authorWen, J-
dc.contributor.authorWu, X-
dc.contributor.authorLi, F-
dc.contributor.authorZhou, Z-
dc.contributor.authorZhu, WG-
dc.contributor.authorLiu, B-
dc.contributor.authorWang, Z-
dc.date.accessioned2019-09-20T08:46:08Z-
dc.date.available2019-09-20T08:46:08Z-
dc.date.issued2019-
dc.identifier.citationScience Advances, 2019, v. 5 n. 3, p. article no. eaav5078-
dc.identifier.issn2375-2548-
dc.identifier.urihttp://hdl.handle.net/10722/277180-
dc.description.abstractDefective 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.-
dc.languageeng-
dc.publisherAmerican Association for the Advancement of Science: Science Advances. The Journal's web site is located at http://www.scienceadvances.org/-
dc.relation.ispartofScience Advances-
dc.rightsThis work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.-
dc.subjectBinding energy-
dc.subjectCell culture-
dc.titleLamin A buffers CK2 kinase activity to modulate aging in a progeria mouse model-
dc.typeArticle-
dc.identifier.emailZhou, Z: zhongjun@hku.hk-
dc.identifier.authorityZhou, Z=rp00503-
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.1126/sciadv.aav5078-
dc.identifier.scopuseid_2-s2.0-85063350991-
dc.identifier.hkuros305496-
dc.identifier.volume5-
dc.identifier.issue3-
dc.identifier.spagearticle no. eaav5078-
dc.identifier.epagearticle no. eaav5078-
dc.publisher.placeUnited States-

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