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csnk1  (New England Biolabs)


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    Structured Review

    New England Biolabs csnk1
    Identification of a novel kinase that phosphorylates SQSTM1 (S349). (A) HeLa cells were treated with rapamycin (MTORC1 inhibitor, 1 µM), CKI-7 <t>(CSNK1</t> and SGK inhibitor, 100 µM), TBCA (CSNK2 inhibitor, 25 µM), rapamycin and CKI-7, or rapamycin and TBCA, together with MG132 (10 µM). Cell lysates were subjected to immunoblot analysis after 12 h. Band intensities were measured, and phosphorylated-SQSTM1 values were normalized to total SQSTM1. The data are reported as means ± SD ( n = 4). Statistical analyses were performed using one-way ANOVA, followed by the Tukey post-hoc test. * P < 0.01. (B) The dual and triple combination treatments of kinase inhibitors were further examined as described in A. Band intensities of S349-phosphorylated SQSTM1 were measured, and the data are reported as means ± SD ( n = 4). Statistical analyses were performed using one-way ANOVA, followed by the Tukey post-hoc test. * P < 0.01. (C) Immunoprecipitates of SQSTM1-mycHis (WT, S349A, and S403A) were incubated with CSNK1 or CSNK2 for 1 h, followed by immunoblot analysis using anti-phosphorylated SQSTM1 (p-SQSTM1 [S349] and p-SQSTM1 [S403]) and anti-SQSTM1 antibodies. (D) Colocalization of SQSTM1 with ubiquitinated inclusions was examined when SQSTM1 (S349)-phosphorylation was inhibited by the treatment with kinase inhibitors (1 µM rapamycin, 100 µM CKI-7, and 25 µM TBCA). Immunocytochemical analysis was performed 12 h after treatment. Cell nuclei were counterstained blue with DAPI. Scale bar: 10 μm.
    Csnk1, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 86 stars, based on 1 article reviews
    csnk1 - by Bioz Stars, 2026-02
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    Images

    1) Product Images from "HSF1 stress response pathway regulates autophagy receptor SQSTM1/p62-associated proteostasis"

    Article Title: HSF1 stress response pathway regulates autophagy receptor SQSTM1/p62-associated proteostasis

    Journal: Autophagy

    doi: 10.1080/15548627.2016.1248018

    Identification of a novel kinase that phosphorylates SQSTM1 (S349). (A) HeLa cells were treated with rapamycin (MTORC1 inhibitor, 1 µM), CKI-7 (CSNK1 and SGK inhibitor, 100 µM), TBCA (CSNK2 inhibitor, 25 µM), rapamycin and CKI-7, or rapamycin and TBCA, together with MG132 (10 µM). Cell lysates were subjected to immunoblot analysis after 12 h. Band intensities were measured, and phosphorylated-SQSTM1 values were normalized to total SQSTM1. The data are reported as means ± SD ( n = 4). Statistical analyses were performed using one-way ANOVA, followed by the Tukey post-hoc test. * P < 0.01. (B) The dual and triple combination treatments of kinase inhibitors were further examined as described in A. Band intensities of S349-phosphorylated SQSTM1 were measured, and the data are reported as means ± SD ( n = 4). Statistical analyses were performed using one-way ANOVA, followed by the Tukey post-hoc test. * P < 0.01. (C) Immunoprecipitates of SQSTM1-mycHis (WT, S349A, and S403A) were incubated with CSNK1 or CSNK2 for 1 h, followed by immunoblot analysis using anti-phosphorylated SQSTM1 (p-SQSTM1 [S349] and p-SQSTM1 [S403]) and anti-SQSTM1 antibodies. (D) Colocalization of SQSTM1 with ubiquitinated inclusions was examined when SQSTM1 (S349)-phosphorylation was inhibited by the treatment with kinase inhibitors (1 µM rapamycin, 100 µM CKI-7, and 25 µM TBCA). Immunocytochemical analysis was performed 12 h after treatment. Cell nuclei were counterstained blue with DAPI. Scale bar: 10 μm.
    Figure Legend Snippet: Identification of a novel kinase that phosphorylates SQSTM1 (S349). (A) HeLa cells were treated with rapamycin (MTORC1 inhibitor, 1 µM), CKI-7 (CSNK1 and SGK inhibitor, 100 µM), TBCA (CSNK2 inhibitor, 25 µM), rapamycin and CKI-7, or rapamycin and TBCA, together with MG132 (10 µM). Cell lysates were subjected to immunoblot analysis after 12 h. Band intensities were measured, and phosphorylated-SQSTM1 values were normalized to total SQSTM1. The data are reported as means ± SD ( n = 4). Statistical analyses were performed using one-way ANOVA, followed by the Tukey post-hoc test. * P < 0.01. (B) The dual and triple combination treatments of kinase inhibitors were further examined as described in A. Band intensities of S349-phosphorylated SQSTM1 were measured, and the data are reported as means ± SD ( n = 4). Statistical analyses were performed using one-way ANOVA, followed by the Tukey post-hoc test. * P < 0.01. (C) Immunoprecipitates of SQSTM1-mycHis (WT, S349A, and S403A) were incubated with CSNK1 or CSNK2 for 1 h, followed by immunoblot analysis using anti-phosphorylated SQSTM1 (p-SQSTM1 [S349] and p-SQSTM1 [S403]) and anti-SQSTM1 antibodies. (D) Colocalization of SQSTM1 with ubiquitinated inclusions was examined when SQSTM1 (S349)-phosphorylation was inhibited by the treatment with kinase inhibitors (1 µM rapamycin, 100 µM CKI-7, and 25 µM TBCA). Immunocytochemical analysis was performed 12 h after treatment. Cell nuclei were counterstained blue with DAPI. Scale bar: 10 μm.

    Techniques Used: Western Blot, Incubation

    Schematic model of the proteostasis network via the HSF1-SQSTM1 axis. HSF1 is activated by the accumulation of harmful proteins, resulting in the induction of cytoprotective genes including HSPs. Moreover, phosphorylation of SQSTM1 by MTORC1, CSNK1, and TBK1 is also induced via activation of HSF1. Phosphorylated SQSTM1 accelerates inclusion formation and autophagic clearance of harmful proteins.
    Figure Legend Snippet: Schematic model of the proteostasis network via the HSF1-SQSTM1 axis. HSF1 is activated by the accumulation of harmful proteins, resulting in the induction of cytoprotective genes including HSPs. Moreover, phosphorylation of SQSTM1 by MTORC1, CSNK1, and TBK1 is also induced via activation of HSF1. Phosphorylated SQSTM1 accelerates inclusion formation and autophagic clearance of harmful proteins.

    Techniques Used: Activation Assay



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    Identification of a novel kinase that phosphorylates SQSTM1 (S349). (A) HeLa cells were treated with rapamycin (MTORC1 inhibitor, 1 µM), CKI-7 <t>(CSNK1</t> and SGK inhibitor, 100 µM), TBCA (CSNK2 inhibitor, 25 µM), rapamycin and CKI-7, or rapamycin and TBCA, together with MG132 (10 µM). Cell lysates were subjected to immunoblot analysis after 12 h. Band intensities were measured, and phosphorylated-SQSTM1 values were normalized to total SQSTM1. The data are reported as means ± SD ( n = 4). Statistical analyses were performed using one-way ANOVA, followed by the Tukey post-hoc test. * P < 0.01. (B) The dual and triple combination treatments of kinase inhibitors were further examined as described in A. Band intensities of S349-phosphorylated SQSTM1 were measured, and the data are reported as means ± SD ( n = 4). Statistical analyses were performed using one-way ANOVA, followed by the Tukey post-hoc test. * P < 0.01. (C) Immunoprecipitates of SQSTM1-mycHis (WT, S349A, and S403A) were incubated with CSNK1 or CSNK2 for 1 h, followed by immunoblot analysis using anti-phosphorylated SQSTM1 (p-SQSTM1 [S349] and p-SQSTM1 [S403]) and anti-SQSTM1 antibodies. (D) Colocalization of SQSTM1 with ubiquitinated inclusions was examined when SQSTM1 (S349)-phosphorylation was inhibited by the treatment with kinase inhibitors (1 µM rapamycin, 100 µM CKI-7, and 25 µM TBCA). Immunocytochemical analysis was performed 12 h after treatment. Cell nuclei were counterstained blue with DAPI. Scale bar: 10 μm.
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    Identification of a novel kinase that phosphorylates SQSTM1 (S349). (A) HeLa cells were treated with rapamycin (MTORC1 inhibitor, 1 µM), CKI-7 <t>(CSNK1</t> and SGK inhibitor, 100 µM), TBCA (CSNK2 inhibitor, 25 µM), rapamycin and CKI-7, or rapamycin and TBCA, together with MG132 (10 µM). Cell lysates were subjected to immunoblot analysis after 12 h. Band intensities were measured, and phosphorylated-SQSTM1 values were normalized to total SQSTM1. The data are reported as means ± SD ( n = 4). Statistical analyses were performed using one-way ANOVA, followed by the Tukey post-hoc test. * P < 0.01. (B) The dual and triple combination treatments of kinase inhibitors were further examined as described in A. Band intensities of S349-phosphorylated SQSTM1 were measured, and the data are reported as means ± SD ( n = 4). Statistical analyses were performed using one-way ANOVA, followed by the Tukey post-hoc test. * P < 0.01. (C) Immunoprecipitates of SQSTM1-mycHis (WT, S349A, and S403A) were incubated with CSNK1 or CSNK2 for 1 h, followed by immunoblot analysis using anti-phosphorylated SQSTM1 (p-SQSTM1 [S349] and p-SQSTM1 [S403]) and anti-SQSTM1 antibodies. (D) Colocalization of SQSTM1 with ubiquitinated inclusions was examined when SQSTM1 (S349)-phosphorylation was inhibited by the treatment with kinase inhibitors (1 µM rapamycin, 100 µM CKI-7, and 25 µM TBCA). Immunocytochemical analysis was performed 12 h after treatment. Cell nuclei were counterstained blue with DAPI. Scale bar: 10 μm.
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    Identification of a novel kinase that phosphorylates SQSTM1 (S349). (A) HeLa cells were treated with rapamycin (MTORC1 inhibitor, 1 µM), CKI-7 <t>(CSNK1</t> and SGK inhibitor, 100 µM), TBCA (CSNK2 inhibitor, 25 µM), rapamycin and CKI-7, or rapamycin and TBCA, together with MG132 (10 µM). Cell lysates were subjected to immunoblot analysis after 12 h. Band intensities were measured, and phosphorylated-SQSTM1 values were normalized to total SQSTM1. The data are reported as means ± SD ( n = 4). Statistical analyses were performed using one-way ANOVA, followed by the Tukey post-hoc test. * P < 0.01. (B) The dual and triple combination treatments of kinase inhibitors were further examined as described in A. Band intensities of S349-phosphorylated SQSTM1 were measured, and the data are reported as means ± SD ( n = 4). Statistical analyses were performed using one-way ANOVA, followed by the Tukey post-hoc test. * P < 0.01. (C) Immunoprecipitates of SQSTM1-mycHis (WT, S349A, and S403A) were incubated with CSNK1 or CSNK2 for 1 h, followed by immunoblot analysis using anti-phosphorylated SQSTM1 (p-SQSTM1 [S349] and p-SQSTM1 [S403]) and anti-SQSTM1 antibodies. (D) Colocalization of SQSTM1 with ubiquitinated inclusions was examined when SQSTM1 (S349)-phosphorylation was inhibited by the treatment with kinase inhibitors (1 µM rapamycin, 100 µM CKI-7, and 25 µM TBCA). Immunocytochemical analysis was performed 12 h after treatment. Cell nuclei were counterstained blue with DAPI. Scale bar: 10 μm.
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    Image Search Results


    Reagents and tools table

    Journal: The EMBO Journal

    Article Title: The global phosphorylation landscape of mouse oocytes during meiotic maturation

    doi: 10.1038/s44318-024-00222-1

    Figure Lengend Snippet: Reagents and tools table

    Article Snippet: CSNK1-IN-1 , MCE , Cat# HY148489.

    Techniques: Virus, Isolation, Reverse Transcription, Purification, SYBR Green Assay, Western Blot, Silver Staining, Sequencing, Over Expression, Recombinant, Plasmid Preparation, Mutagenesis, Software

    Identification of a novel kinase that phosphorylates SQSTM1 (S349). (A) HeLa cells were treated with rapamycin (MTORC1 inhibitor, 1 µM), CKI-7 (CSNK1 and SGK inhibitor, 100 µM), TBCA (CSNK2 inhibitor, 25 µM), rapamycin and CKI-7, or rapamycin and TBCA, together with MG132 (10 µM). Cell lysates were subjected to immunoblot analysis after 12 h. Band intensities were measured, and phosphorylated-SQSTM1 values were normalized to total SQSTM1. The data are reported as means ± SD ( n = 4). Statistical analyses were performed using one-way ANOVA, followed by the Tukey post-hoc test. * P < 0.01. (B) The dual and triple combination treatments of kinase inhibitors were further examined as described in A. Band intensities of S349-phosphorylated SQSTM1 were measured, and the data are reported as means ± SD ( n = 4). Statistical analyses were performed using one-way ANOVA, followed by the Tukey post-hoc test. * P < 0.01. (C) Immunoprecipitates of SQSTM1-mycHis (WT, S349A, and S403A) were incubated with CSNK1 or CSNK2 for 1 h, followed by immunoblot analysis using anti-phosphorylated SQSTM1 (p-SQSTM1 [S349] and p-SQSTM1 [S403]) and anti-SQSTM1 antibodies. (D) Colocalization of SQSTM1 with ubiquitinated inclusions was examined when SQSTM1 (S349)-phosphorylation was inhibited by the treatment with kinase inhibitors (1 µM rapamycin, 100 µM CKI-7, and 25 µM TBCA). Immunocytochemical analysis was performed 12 h after treatment. Cell nuclei were counterstained blue with DAPI. Scale bar: 10 μm.

    Journal: Autophagy

    Article Title: HSF1 stress response pathway regulates autophagy receptor SQSTM1/p62-associated proteostasis

    doi: 10.1080/15548627.2016.1248018

    Figure Lengend Snippet: Identification of a novel kinase that phosphorylates SQSTM1 (S349). (A) HeLa cells were treated with rapamycin (MTORC1 inhibitor, 1 µM), CKI-7 (CSNK1 and SGK inhibitor, 100 µM), TBCA (CSNK2 inhibitor, 25 µM), rapamycin and CKI-7, or rapamycin and TBCA, together with MG132 (10 µM). Cell lysates were subjected to immunoblot analysis after 12 h. Band intensities were measured, and phosphorylated-SQSTM1 values were normalized to total SQSTM1. The data are reported as means ± SD ( n = 4). Statistical analyses were performed using one-way ANOVA, followed by the Tukey post-hoc test. * P < 0.01. (B) The dual and triple combination treatments of kinase inhibitors were further examined as described in A. Band intensities of S349-phosphorylated SQSTM1 were measured, and the data are reported as means ± SD ( n = 4). Statistical analyses were performed using one-way ANOVA, followed by the Tukey post-hoc test. * P < 0.01. (C) Immunoprecipitates of SQSTM1-mycHis (WT, S349A, and S403A) were incubated with CSNK1 or CSNK2 for 1 h, followed by immunoblot analysis using anti-phosphorylated SQSTM1 (p-SQSTM1 [S349] and p-SQSTM1 [S403]) and anti-SQSTM1 antibodies. (D) Colocalization of SQSTM1 with ubiquitinated inclusions was examined when SQSTM1 (S349)-phosphorylation was inhibited by the treatment with kinase inhibitors (1 µM rapamycin, 100 µM CKI-7, and 25 µM TBCA). Immunocytochemical analysis was performed 12 h after treatment. Cell nuclei were counterstained blue with DAPI. Scale bar: 10 μm.

    Article Snippet: A reaction buffer containing 1 mM ATP was added to immunoprecipitation products, and then the mixtures were incubated with or without 1000 units of CSNK1 (New England Biolabs, P6030S) or 500 units of CSNK2 (New England Biolabs, P6010S) for 1 h at 37°C.

    Techniques: Western Blot, Incubation

    Schematic model of the proteostasis network via the HSF1-SQSTM1 axis. HSF1 is activated by the accumulation of harmful proteins, resulting in the induction of cytoprotective genes including HSPs. Moreover, phosphorylation of SQSTM1 by MTORC1, CSNK1, and TBK1 is also induced via activation of HSF1. Phosphorylated SQSTM1 accelerates inclusion formation and autophagic clearance of harmful proteins.

    Journal: Autophagy

    Article Title: HSF1 stress response pathway regulates autophagy receptor SQSTM1/p62-associated proteostasis

    doi: 10.1080/15548627.2016.1248018

    Figure Lengend Snippet: Schematic model of the proteostasis network via the HSF1-SQSTM1 axis. HSF1 is activated by the accumulation of harmful proteins, resulting in the induction of cytoprotective genes including HSPs. Moreover, phosphorylation of SQSTM1 by MTORC1, CSNK1, and TBK1 is also induced via activation of HSF1. Phosphorylated SQSTM1 accelerates inclusion formation and autophagic clearance of harmful proteins.

    Article Snippet: A reaction buffer containing 1 mM ATP was added to immunoprecipitation products, and then the mixtures were incubated with or without 1000 units of CSNK1 (New England Biolabs, P6030S) or 500 units of CSNK2 (New England Biolabs, P6010S) for 1 h at 37°C.

    Techniques: Activation Assay