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pegfr y1045  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc pegfr y1045
    C. albicans induces EGFR phosphorylation at <t>Y1045</t> and EGFR ubiquitination in TR146 oral epithelial cells in an ECE1 -driven manner. ( A ) Schematic of EGFR phosphorylation and ubiquitination. Created with BioRender.com. ( B ) TR146 cells were infected with wild-type (WT) C. albicans (BWP17), an ECE1 null strain ( ece1 Δ/Δ), an ECE1 re-integrant strain ( ece1 Δ/Δ + ECE1 ), or a candidalysin null strain ( ece1 Δ/Δ + ECE1 Δ184–279 ) for 4 h at an MOI of 10 or stimulated with PBS as a vehicle control. Lysates (10 µg) were electrophoresed on gradient gels to detect pEGFR Y1045 and α-actin via Western blot. Data are representative of three independent experiments. ( C ) TR146 cells were infected with WT C. albicans (SC5314), ece1 Δ/Δ, ece1 Δ/Δ + ECE1 , ece1 Δ/Δ+ ECE1 Δ184–279 , and als3 Δ/Δ for 6 h at an MOI of 5 or stimulated with PBS as a vehicle control. EGF 100 ng/mL was used as a positive control. Lysates were collected and EGFR was immunoprecipitated. Immunoprecipitation (IP) samples were electrophoresed on gradient gels to detect total EGFR and ubiquitin via Western blot. Data are representative of three independent experiments. Dashed vertical lines indicate omitted, extraneous portions of blot images. ( D ) Relative protein levels in panel C were quantified using densitometry. Ubiquitin was normalized to total EGFR and expressed relative to the control (PBS), which was set to 1. Data represent the average of three to seven independent experiments and are presented as mean values with standard error of the mean (SEM) error bars. Statistical significance was determined using the Kruskal–Wallis test with Dunn’s multiple comparison test. P < 0.05, *** P < 0.001. ( E ) TR146 cells were infected with WT C. albicans (SC5314), ece1 Δ/Δ, and als3 Δ/Δ for 6 h at an MOI of 5 or stimulated with PBS as a vehicle control. Lysates were collected and EGFR was immunoprecipitated. IP samples were electrophoresed on gradient gels to detect total EGFR, Grb2, AP2M1, and HRS via Western blot. Dashed vertical lines indicate omitted, extraneous portions of blot images. Data are representative of three independent experiments. ( F–H ) Relative protein levels in panel E were quantified using densitometry. Grb2, AP2M1, and HRS were normalized to total EGFR and expressed relative to the control (PBS), which was set to 1. Data represent the average of three to four independent experiments and are presented as mean values with SEM error bars. Statistical significance was determined using a parametric test (ordinary one-way ANOVA with Dunnett’s multiple comparison test). * P < 0.05. ns, not significant.
    Pegfr Y1045, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/pegfr+y1045/pmc12892998-13-0-7?v=Cell+Signaling+Technology+Inc
    Average 86 stars, based on 1 article reviews
    pegfr y1045 - by Bioz Stars, 2026-08
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    Images

    1) Product Images from "Candida albicans -induced ubiquitination of EGFR reveals novel host–fungal interaction pathways"

    Article Title: Candida albicans -induced ubiquitination of EGFR reveals novel host–fungal interaction pathways

    Journal: mBio

    doi: 10.1128/mbio.03448-25

    C. albicans induces EGFR phosphorylation at Y1045 and EGFR ubiquitination in TR146 oral epithelial cells in an ECE1 -driven manner. ( A ) Schematic of EGFR phosphorylation and ubiquitination. Created with BioRender.com. ( B ) TR146 cells were infected with wild-type (WT) C. albicans (BWP17), an ECE1 null strain ( ece1 Δ/Δ), an ECE1 re-integrant strain ( ece1 Δ/Δ + ECE1 ), or a candidalysin null strain ( ece1 Δ/Δ + ECE1 Δ184–279 ) for 4 h at an MOI of 10 or stimulated with PBS as a vehicle control. Lysates (10 µg) were electrophoresed on gradient gels to detect pEGFR Y1045 and α-actin via Western blot. Data are representative of three independent experiments. ( C ) TR146 cells were infected with WT C. albicans (SC5314), ece1 Δ/Δ, ece1 Δ/Δ + ECE1 , ece1 Δ/Δ+ ECE1 Δ184–279 , and als3 Δ/Δ for 6 h at an MOI of 5 or stimulated with PBS as a vehicle control. EGF 100 ng/mL was used as a positive control. Lysates were collected and EGFR was immunoprecipitated. Immunoprecipitation (IP) samples were electrophoresed on gradient gels to detect total EGFR and ubiquitin via Western blot. Data are representative of three independent experiments. Dashed vertical lines indicate omitted, extraneous portions of blot images. ( D ) Relative protein levels in panel C were quantified using densitometry. Ubiquitin was normalized to total EGFR and expressed relative to the control (PBS), which was set to 1. Data represent the average of three to seven independent experiments and are presented as mean values with standard error of the mean (SEM) error bars. Statistical significance was determined using the Kruskal–Wallis test with Dunn’s multiple comparison test. P < 0.05, *** P < 0.001. ( E ) TR146 cells were infected with WT C. albicans (SC5314), ece1 Δ/Δ, and als3 Δ/Δ for 6 h at an MOI of 5 or stimulated with PBS as a vehicle control. Lysates were collected and EGFR was immunoprecipitated. IP samples were electrophoresed on gradient gels to detect total EGFR, Grb2, AP2M1, and HRS via Western blot. Dashed vertical lines indicate omitted, extraneous portions of blot images. Data are representative of three independent experiments. ( F–H ) Relative protein levels in panel E were quantified using densitometry. Grb2, AP2M1, and HRS were normalized to total EGFR and expressed relative to the control (PBS), which was set to 1. Data represent the average of three to four independent experiments and are presented as mean values with SEM error bars. Statistical significance was determined using a parametric test (ordinary one-way ANOVA with Dunnett’s multiple comparison test). * P < 0.05. ns, not significant.
    Figure Legend Snippet: C. albicans induces EGFR phosphorylation at Y1045 and EGFR ubiquitination in TR146 oral epithelial cells in an ECE1 -driven manner. ( A ) Schematic of EGFR phosphorylation and ubiquitination. Created with BioRender.com. ( B ) TR146 cells were infected with wild-type (WT) C. albicans (BWP17), an ECE1 null strain ( ece1 Δ/Δ), an ECE1 re-integrant strain ( ece1 Δ/Δ + ECE1 ), or a candidalysin null strain ( ece1 Δ/Δ + ECE1 Δ184–279 ) for 4 h at an MOI of 10 or stimulated with PBS as a vehicle control. Lysates (10 µg) were electrophoresed on gradient gels to detect pEGFR Y1045 and α-actin via Western blot. Data are representative of three independent experiments. ( C ) TR146 cells were infected with WT C. albicans (SC5314), ece1 Δ/Δ, ece1 Δ/Δ + ECE1 , ece1 Δ/Δ+ ECE1 Δ184–279 , and als3 Δ/Δ for 6 h at an MOI of 5 or stimulated with PBS as a vehicle control. EGF 100 ng/mL was used as a positive control. Lysates were collected and EGFR was immunoprecipitated. Immunoprecipitation (IP) samples were electrophoresed on gradient gels to detect total EGFR and ubiquitin via Western blot. Data are representative of three independent experiments. Dashed vertical lines indicate omitted, extraneous portions of blot images. ( D ) Relative protein levels in panel C were quantified using densitometry. Ubiquitin was normalized to total EGFR and expressed relative to the control (PBS), which was set to 1. Data represent the average of three to seven independent experiments and are presented as mean values with standard error of the mean (SEM) error bars. Statistical significance was determined using the Kruskal–Wallis test with Dunn’s multiple comparison test. P < 0.05, *** P < 0.001. ( E ) TR146 cells were infected with WT C. albicans (SC5314), ece1 Δ/Δ, and als3 Δ/Δ for 6 h at an MOI of 5 or stimulated with PBS as a vehicle control. Lysates were collected and EGFR was immunoprecipitated. IP samples were electrophoresed on gradient gels to detect total EGFR, Grb2, AP2M1, and HRS via Western blot. Dashed vertical lines indicate omitted, extraneous portions of blot images. Data are representative of three independent experiments. ( F–H ) Relative protein levels in panel E were quantified using densitometry. Grb2, AP2M1, and HRS were normalized to total EGFR and expressed relative to the control (PBS), which was set to 1. Data represent the average of three to four independent experiments and are presented as mean values with SEM error bars. Statistical significance was determined using a parametric test (ordinary one-way ANOVA with Dunnett’s multiple comparison test). * P < 0.05. ns, not significant.

    Techniques Used: Phospho-proteomics, Ubiquitin Proteomics, Infection, Control, Western Blot, Positive Control, Immunoprecipitation, Comparison



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    C. albicans induces EGFR phosphorylation at <t>Y1045</t> and EGFR ubiquitination in TR146 oral epithelial cells in an ECE1 -driven manner. ( A ) Schematic of EGFR phosphorylation and ubiquitination. Created with BioRender.com. ( B ) TR146 cells were infected with wild-type (WT) C. albicans (BWP17), an ECE1 null strain ( ece1 Δ/Δ), an ECE1 re-integrant strain ( ece1 Δ/Δ + ECE1 ), or a candidalysin null strain ( ece1 Δ/Δ + ECE1 Δ184–279 ) for 4 h at an MOI of 10 or stimulated with PBS as a vehicle control. Lysates (10 µg) were electrophoresed on gradient gels to detect pEGFR Y1045 and α-actin via Western blot. Data are representative of three independent experiments. ( C ) TR146 cells were infected with WT C. albicans (SC5314), ece1 Δ/Δ, ece1 Δ/Δ + ECE1 , ece1 Δ/Δ+ ECE1 Δ184–279 , and als3 Δ/Δ for 6 h at an MOI of 5 or stimulated with PBS as a vehicle control. EGF 100 ng/mL was used as a positive control. Lysates were collected and EGFR was immunoprecipitated. Immunoprecipitation (IP) samples were electrophoresed on gradient gels to detect total EGFR and ubiquitin via Western blot. Data are representative of three independent experiments. Dashed vertical lines indicate omitted, extraneous portions of blot images. ( D ) Relative protein levels in panel C were quantified using densitometry. Ubiquitin was normalized to total EGFR and expressed relative to the control (PBS), which was set to 1. Data represent the average of three to seven independent experiments and are presented as mean values with standard error of the mean (SEM) error bars. Statistical significance was determined using the Kruskal–Wallis test with Dunn’s multiple comparison test. P < 0.05, *** P < 0.001. ( E ) TR146 cells were infected with WT C. albicans (SC5314), ece1 Δ/Δ, and als3 Δ/Δ for 6 h at an MOI of 5 or stimulated with PBS as a vehicle control. Lysates were collected and EGFR was immunoprecipitated. IP samples were electrophoresed on gradient gels to detect total EGFR, Grb2, AP2M1, and HRS via Western blot. Dashed vertical lines indicate omitted, extraneous portions of blot images. Data are representative of three independent experiments. ( F–H ) Relative protein levels in panel E were quantified using densitometry. Grb2, AP2M1, and HRS were normalized to total EGFR and expressed relative to the control (PBS), which was set to 1. Data represent the average of three to four independent experiments and are presented as mean values with SEM error bars. Statistical significance was determined using a parametric test (ordinary one-way ANOVA with Dunnett’s multiple comparison test). * P < 0.05. ns, not significant.
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    Image Search Results


    C. albicans induces EGFR phosphorylation at Y1045 and EGFR ubiquitination in TR146 oral epithelial cells in an ECE1 -driven manner. ( A ) Schematic of EGFR phosphorylation and ubiquitination. Created with BioRender.com. ( B ) TR146 cells were infected with wild-type (WT) C. albicans (BWP17), an ECE1 null strain ( ece1 Δ/Δ), an ECE1 re-integrant strain ( ece1 Δ/Δ + ECE1 ), or a candidalysin null strain ( ece1 Δ/Δ + ECE1 Δ184–279 ) for 4 h at an MOI of 10 or stimulated with PBS as a vehicle control. Lysates (10 µg) were electrophoresed on gradient gels to detect pEGFR Y1045 and α-actin via Western blot. Data are representative of three independent experiments. ( C ) TR146 cells were infected with WT C. albicans (SC5314), ece1 Δ/Δ, ece1 Δ/Δ + ECE1 , ece1 Δ/Δ+ ECE1 Δ184–279 , and als3 Δ/Δ for 6 h at an MOI of 5 or stimulated with PBS as a vehicle control. EGF 100 ng/mL was used as a positive control. Lysates were collected and EGFR was immunoprecipitated. Immunoprecipitation (IP) samples were electrophoresed on gradient gels to detect total EGFR and ubiquitin via Western blot. Data are representative of three independent experiments. Dashed vertical lines indicate omitted, extraneous portions of blot images. ( D ) Relative protein levels in panel C were quantified using densitometry. Ubiquitin was normalized to total EGFR and expressed relative to the control (PBS), which was set to 1. Data represent the average of three to seven independent experiments and are presented as mean values with standard error of the mean (SEM) error bars. Statistical significance was determined using the Kruskal–Wallis test with Dunn’s multiple comparison test. P < 0.05, *** P < 0.001. ( E ) TR146 cells were infected with WT C. albicans (SC5314), ece1 Δ/Δ, and als3 Δ/Δ for 6 h at an MOI of 5 or stimulated with PBS as a vehicle control. Lysates were collected and EGFR was immunoprecipitated. IP samples were electrophoresed on gradient gels to detect total EGFR, Grb2, AP2M1, and HRS via Western blot. Dashed vertical lines indicate omitted, extraneous portions of blot images. Data are representative of three independent experiments. ( F–H ) Relative protein levels in panel E were quantified using densitometry. Grb2, AP2M1, and HRS were normalized to total EGFR and expressed relative to the control (PBS), which was set to 1. Data represent the average of three to four independent experiments and are presented as mean values with SEM error bars. Statistical significance was determined using a parametric test (ordinary one-way ANOVA with Dunnett’s multiple comparison test). * P < 0.05. ns, not significant.

    Journal: mBio

    Article Title: Candida albicans -induced ubiquitination of EGFR reveals novel host–fungal interaction pathways

    doi: 10.1128/mbio.03448-25

    Figure Lengend Snippet: C. albicans induces EGFR phosphorylation at Y1045 and EGFR ubiquitination in TR146 oral epithelial cells in an ECE1 -driven manner. ( A ) Schematic of EGFR phosphorylation and ubiquitination. Created with BioRender.com. ( B ) TR146 cells were infected with wild-type (WT) C. albicans (BWP17), an ECE1 null strain ( ece1 Δ/Δ), an ECE1 re-integrant strain ( ece1 Δ/Δ + ECE1 ), or a candidalysin null strain ( ece1 Δ/Δ + ECE1 Δ184–279 ) for 4 h at an MOI of 10 or stimulated with PBS as a vehicle control. Lysates (10 µg) were electrophoresed on gradient gels to detect pEGFR Y1045 and α-actin via Western blot. Data are representative of three independent experiments. ( C ) TR146 cells were infected with WT C. albicans (SC5314), ece1 Δ/Δ, ece1 Δ/Δ + ECE1 , ece1 Δ/Δ+ ECE1 Δ184–279 , and als3 Δ/Δ for 6 h at an MOI of 5 or stimulated with PBS as a vehicle control. EGF 100 ng/mL was used as a positive control. Lysates were collected and EGFR was immunoprecipitated. Immunoprecipitation (IP) samples were electrophoresed on gradient gels to detect total EGFR and ubiquitin via Western blot. Data are representative of three independent experiments. Dashed vertical lines indicate omitted, extraneous portions of blot images. ( D ) Relative protein levels in panel C were quantified using densitometry. Ubiquitin was normalized to total EGFR and expressed relative to the control (PBS), which was set to 1. Data represent the average of three to seven independent experiments and are presented as mean values with standard error of the mean (SEM) error bars. Statistical significance was determined using the Kruskal–Wallis test with Dunn’s multiple comparison test. P < 0.05, *** P < 0.001. ( E ) TR146 cells were infected with WT C. albicans (SC5314), ece1 Δ/Δ, and als3 Δ/Δ for 6 h at an MOI of 5 or stimulated with PBS as a vehicle control. Lysates were collected and EGFR was immunoprecipitated. IP samples were electrophoresed on gradient gels to detect total EGFR, Grb2, AP2M1, and HRS via Western blot. Dashed vertical lines indicate omitted, extraneous portions of blot images. Data are representative of three independent experiments. ( F–H ) Relative protein levels in panel E were quantified using densitometry. Grb2, AP2M1, and HRS were normalized to total EGFR and expressed relative to the control (PBS), which was set to 1. Data represent the average of three to four independent experiments and are presented as mean values with SEM error bars. Statistical significance was determined using a parametric test (ordinary one-way ANOVA with Dunnett’s multiple comparison test). * P < 0.05. ns, not significant.

    Article Snippet: pEGFR Y1045 , Rabbit , 1:1,000 , Cell Signaling Technology , 2237.

    Techniques: Phospho-proteomics, Ubiquitin Proteomics, Infection, Control, Western Blot, Positive Control, Immunoprecipitation, Comparison