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Cited by 78

The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.

Autophagy-dependent senescence in response to DNA damage and chronic apoptotic stress

Singh, Kamini, Matsuyama, Shigemi, Drazba, Judith A., Almasan, Alexandru·2012·Autophagy
DOI 10.4161/auto.8.2.18600
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Abstract

Autophagy regulates cell survival and cell death upon various cellular stresses, yet the molecular signaling events involved are not well defined. Here, we established the function of a proteolytic Cyclin E fragment (p18-CycE) in DNA damage-induced autophagy, apoptosis, and senescence. p18-CycE was identified in hematopoietic cells undergoing DNA damage-induced apoptosis. In epithelial cells exposed to DNA damage, chronic but not transient expression of p18-CycE leads to higher turnover of LC3 I/II and increased emergence of autophagosomes and autolysosomes. Levels of p18-CycE, which was generated by proteolytic cleavage of endogenous Cyclin E, were greatly increased by chloroquine and correlated with LC 3II conversion. Preventing p18-CycE genesis blocked conversion of LC3 I to LC3 II. Upon DNA damage, cytoplasmic ataxia-telangiectasia-mutated (ATM) was phosphorylated in p18-CycE-expressing cells resulting in sustained activation of the adenosine-mono-phosphate-dependent kinase (AMPK). These lead to sustained activation of mammalian autophagy-initiating kinase ULK1, which was abrogated upon inhibiting ATM and AMPK phosphorylation. Moreover, p18-CycE was degraded via autophagy followed by induction of senescence. Both autophagy and senescence were prevented by inhibiting autophagy, which leads to increased apoptosis in p18-CycE-expressing cells by stabilizing p18-CycE expression. Senescence was further associated with cytoplasmic co-localization and degradation of p18-CycE and…

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Crossref · 10.4161/auto.8.2.18600

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8 of 8 references verified0 citation errors · 0 not checkable

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Claims other papers make about this one

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  • UNC-51 is not required for the clearance of neuroblast corpses in larval worms or released cell fragments in worm embryos.

    “UNC-51 (the Atg1/ULK1 homolog in C. elegans) is not required for the clearance of neuroblast corpses in larval worms or released cell fragments in worm embryos [752, 753]”

    From Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1 (2021) · cites this paper as [752]

Citations

Cites

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Research works printed but not linked: 32

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Metadata

Authors
Singh, K., Matsuyama, S., Drazba, J. A., & Almasan, A.
Affiliations
  • Department of Cancer Biology; Lerner Research Institute; Cleveland Clinic; Cleveland, OH USA
  • Department of Medicine; Division of Hematology/Oncology; Case Western Reserve University; Cleveland, OH USA
  • Imaging Core; Lerner Research Institute; Cleveland Clinic; Cleveland, OH USA
Venue
Autophagy
Publisher
Informa UK Limited
Published
2012-02
Volume
8
Issue
2
Pages
236-251
ISSN
  • 1554-8627
  • 1554-8635
DOI
10.4161/auto.8.2.18600
Cited by
78
References
8
Language
en

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