A novel role for YPEL2 in mediating endothelial cellular senescence via the p53/p21 pathway

Xu, Jianxiong; Tang, Mao-Lin; Lu, Zhifeng; Song, Yu; Zhang, Kelan; He, Run-Chao; Guo, Xiangna; Yuan, Yun-Qi; Dai, Xiaoyan; Ma, Xin

doi:10.1016/j.mad.2023.111803

Cited by 3 publications

(2 citation statements)

References 52 publications

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“…Similarly, recent studies showed an increased expression of YPEL2 in human atherosclerotic plaques (J.-X. Xu et al, 2023) and that YPEL2 in response to a stress inducer drives premature senescence of an endothelial cell model by blocking the cell cycle through the activation of the p53/p21 pathway (J.-X. Xu et al, 2023).…”

Section: Discussionmentioning

confidence: 85%

“…Xu et al, 2023) and that YPEL2 in response to a stress inducer drives premature senescence of an endothelial cell model by blocking the cell cycle through the activation of the p53/p21 pathway (J.‐X. Xu et al, 2023). We here observe that inducible synthesis of YPEL2 in COS7 cells, displaying diffuse intracellular staining encompassing both the nucleus and cytoplasm, induces a temporal stalling of cellular proliferation without affecting cell cycle kinetics or cell death.…”

Section: Discussionmentioning

confidence: 99%

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Dynamic proximity interaction profiling suggests that YPEL2 is involved in cellular stress surveillance

Turan,

Olgun,

Ayten

et al. 2024

Protein Science

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YPEL2 is a member of the evolutionarily conserved YPEL family involved in cellular proliferation, mobility, differentiation, senescence, and death. However, the mechanism by which YPEL2, or YPEL proteins, mediates its effects is largely unknown. Proteins perform their functions in a network of proteins whose identities, amounts, and compositions change spatiotemporally in a lineage‐specific manner in response to internal and external stimuli. Here, we explored interaction partners of YPEL2 by using dynamic TurboID‐coupled mass spectrometry analyses to infer a function for the protein. Our results using inducible transgene expressions in COS7 cells indicate that proximity interaction partners of YPEL2 are mainly involved in RNA and mRNA metabolic processes, ribonucleoprotein complex biogenesis, regulation of gene silencing by miRNA, and cellular responses to stress. We showed that YPEL2 interacts with the RNA‐binding protein ELAVL1 and the selective autophagy receptor SQSTM1. We also found that YPEL2 localizes stress granules in response to sodium arsenite, an oxidative stress inducer, which suggests that YPEL2 participates in stress granule‐related processes. Establishing a point of departure in the delineation of structural/functional features of YPEL2, our results suggest that YPEL2 may be involved in stress surveillance mechanisms.This article is protected by copyright. All rights reserved.

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Section: Discussionmentioning

confidence: 85%

Section: Discussionmentioning

confidence: 99%

Dynamic proximity interaction profiling suggests that YPEL2 is involved in cellular stress surveillance

Turan,

Olgun,

Ayten

et al. 2024

Protein Science

View full text Add to dashboard Cite

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CircHIPK3 targets DRP1 to mediate hydrogen peroxide-induced necroptosis of vascular smooth muscle cells and atherosclerotic vulnerable plaque formation

Li,

Yang,

Wang

et al. 2024

Journal of Advanced Research

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Dynamic proximity interaction profiling suggests that YPEL2 is involved in cellular stress surveillance

Turan,

Olgun,

Ayten

et al. 2023

Preprint

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YPEL2 is a member of the evolutionarily conserved YPEL family involved in cellular proliferation, mobility, differentiation as well as senescence and death. However, the mechanism by which YPEL2, or YPEL proteins, mediates its effects is yet unknown. Proteins perform their functions in a network of proteins whose identities, amounts, and compositions change spatiotemporally in a lineage-specific manner in response to internal and external stimuli. We here explored interaction partners of YPEL2 by using dynamic TurboID-coupled mass spectrometry analyses to infer a function for the protein. Our results using inducible transgene expressions in COS7 cells indicate that proximity interaction partners of YPEL2 are largely involved in RNA and mRNA metabolic processes, ribonucleoprotein complex biogenesis, regulation of gene silencing by miRNA, and cellular responses to stress. We showed that YPEL2 interacts with RNA binding protein ELAVL1 and selective autophagy receptor SQSTM1. We also found that YPEL2 participates in events associated with the formation/disassembly of stress granules in response to sodium arsenite an oxidative stress inducer. Establishing a point of departure in the delineation of structural/functional features of YPEL2, our results suggest that YPEL2 may be involved in stress surveillance mechanisms.

show abstract

A novel role for YPEL2 in mediating endothelial cellular senescence via the p53/p21 pathway

Cited by 3 publications

References 52 publications

Dynamic proximity interaction profiling suggests that YPEL2 is involved in cellular stress surveillance

Dynamic proximity interaction profiling suggests that YPEL2 is involved in cellular stress surveillance

CircHIPK3 targets DRP1 to mediate hydrogen peroxide-induced necroptosis of vascular smooth muscle cells and atherosclerotic vulnerable plaque formation

Dynamic proximity interaction profiling suggests that YPEL2 is involved in cellular stress surveillance

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