Deep Insight Into YPEL3

Miller, Kelly Lr; Yelton, Larrilyn

doi:10.4267/2042/62194

Cited by 2 publications

(4 citation statements)

References 13 publications

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“…Likewise, YPEL3 localization is suggested to be weakly nuclear with punctate perinuclear staining (Heminger et al, 2009 ). On the other hand, YPEL3, using a YPEL3‐specific antibody, is reported to show diffuse staining, including nucleus and cytoplasm (Miller & Yelton, 2017 ). The pan‐YPEL antibody we used to detect the Flag‐YPEL proteins in WB analyses reveals staining in un‐transfected COS7 cells encompassing both the cytoplasm and the nucleus as well as denser staining puncta at the nuclear periphery reminiscent of the centrosomic region (Baker, 2003 ) (Figure 2f ).…”

Section: Resultsmentioning

confidence: 99%

“…org/) using the ClustalOmega (Sievers & Higgins, 2021) plug-in (https://www.ebi.ac.uk/Tools/msa/clustalo/). For the tertiary structure prediction and superimposition of the tertiary structures of YPEL1-5 proteins, we used the AlphaFold (Jumper et al, 2021;Varadi et al, 2022) server (https://alphafold.ebi.ac.uk/) with the ChimeraX molecular visualization (Baek et al, 2021;Goddard et al, 2018;Miller & Yelton, 2017;Pettersen et al, 2021) program (https://www.cgl.ucsf.edu/chimerax/). For the homology modeling of YPEL proteins, we used the Phyre2 (L. A.…”

Section: Discussionmentioning

confidence: 99%

“…The alignment of amino acid sequences of human YPEL proteins was generated with the Jalview (Waterhouse et al, 2009 ) program ( https://www.jalview.org/ ) using the ClustalOmega (Sievers & Higgins, 2021 ) plug‐in ( https://www.ebi.ac.uk/Tools/msa/clustalo/ ). For the tertiary structure prediction and superimposition of the tertiary structures of YPEL1‐5 proteins, we used the AlphaFold (Jumper et al, 2021 ; Varadi et al, 2022 ) server ( https://alphafold.ebi.ac.uk/ ) with the ChimeraX molecular visualization (Baek et al, 2021 ; Goddard et al, 2018 ; Miller & Yelton, 2017 ; Pettersen et al, 2021 ) program ( https://www.cgl.ucsf.edu/chimerax/ ). For the homology modeling of YPEL proteins, we used the Phyre2 (L. A. Kelley et al, 2015 ) protein fold recognition server ( http://www.sbg.bio.ic.ac.uk/~phyre2/html/page.cgi?id=index ).…”

Section: Methodsmentioning

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: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

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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“…Similarly, mouse Ypel1 as a GFP-fusion protein is reported to localize to the nucleus in transfected NIH3T3 mouse fibroblast cells 8 . Likewise, YPEL3 localization is suggested to be weakly nuclear with punctate perinuclear staining 81 . On the other hand, YPEL3, using a YPEL3-specific antibody, is reported to show diffuse staining including nucleus and cytoplasm 25 .…”

Section: Resultsmentioning

confidence: 99%

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.

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Deep Insight Into YPEL3

Abstract: Deep insight into YPEL3.

Cited by 2 publications

References 13 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

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

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