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flag  (Proteintech)
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CNH inhibits MAP4K-induced phosphorylation of DVL3. (A) Co-immunoprecipitation results showing the interaction of CNH with DVL3. (B) Co-immunoprecipitation results showing the interaction of DVL3 with HGK, MINK1, or TNIK. (C) The PDZ domain of DVL3 mediates its interaction with MINK1. DIX: homology region between DIshevelled and aXin; PDZ: homology region shared by PSD95, Dlg1, and Zo-1; DEP: shared homology region between Dishevelled, Egl-10, and Pleckstrin domain. (D) Mobility shift of DVL3 induced by wild-type but not kinase-dead (K54R) MAP4Ks. The migration front of the indicated protein bands is marked by a red line. (E) Western blots showing MAP4K-induced threonine phosphorylation of DLV3, which could be largely abolished after treatment with lambda protein phosphatase (λPP). p-Thr, antibody specific for phosphorylated threonine. (F) Phos-tag SDS-PAGE and western blotting to show suppression of HGK-mediated <t>FLAG-DVL3</t> phosphorylation by CNH. (G) Schematic representation of HGK-induced phosphorylation of DVL3. The sites were identified by phospho proteomics. Different color represents relative enrichment of phosphorylation when compared to the control without ectopic HGK. APP: Amyloid precursor protein; CNH: Citron homology domain; Ctrl: control; DVL3: dishevelled segment polarity protein 3; GFP: green fluorescent protein; HA: hemagglutinin; p-Thr: phospho-threonine.
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anti flag  (Proteintech)
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CNH inhibits MAP4K-induced phosphorylation of DVL3. (A) Co-immunoprecipitation results showing the interaction of CNH with DVL3. (B) Co-immunoprecipitation results showing the interaction of DVL3 with HGK, MINK1, or TNIK. (C) The PDZ domain of DVL3 mediates its interaction with MINK1. DIX: homology region between DIshevelled and aXin; PDZ: homology region shared by PSD95, Dlg1, and Zo-1; DEP: shared homology region between Dishevelled, Egl-10, and Pleckstrin domain. (D) Mobility shift of DVL3 induced by wild-type but not kinase-dead (K54R) MAP4Ks. The migration front of the indicated protein bands is marked by a red line. (E) Western blots showing MAP4K-induced threonine phosphorylation of DLV3, which could be largely abolished after treatment with lambda protein phosphatase (λPP). p-Thr, antibody specific for phosphorylated threonine. (F) Phos-tag SDS-PAGE and western blotting to show suppression of HGK-mediated <t>FLAG-DVL3</t> phosphorylation by CNH. (G) Schematic representation of HGK-induced phosphorylation of DVL3. The sites were identified by phospho proteomics. Different color represents relative enrichment of phosphorylation when compared to the control without ectopic HGK. APP: Amyloid precursor protein; CNH: Citron homology domain; Ctrl: control; DVL3: dishevelled segment polarity protein 3; GFP: green fluorescent protein; HA: hemagglutinin; p-Thr: phospho-threonine.
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mouse dykddddk tag  (Cell Signaling Technology Inc)
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CNH inhibits MAP4K-induced phosphorylation of DVL3. (A) Co-immunoprecipitation results showing the interaction of CNH with DVL3. (B) Co-immunoprecipitation results showing the interaction of DVL3 with HGK, MINK1, or TNIK. (C) The PDZ domain of DVL3 mediates its interaction with MINK1. DIX: homology region between DIshevelled and aXin; PDZ: homology region shared by PSD95, Dlg1, and Zo-1; DEP: shared homology region between Dishevelled, Egl-10, and Pleckstrin domain. (D) Mobility shift of DVL3 induced by wild-type but not kinase-dead (K54R) MAP4Ks. The migration front of the indicated protein bands is marked by a red line. (E) Western blots showing MAP4K-induced threonine phosphorylation of DLV3, which could be largely abolished after treatment with lambda protein phosphatase (λPP). p-Thr, antibody specific for phosphorylated threonine. (F) Phos-tag SDS-PAGE and western blotting to show suppression of HGK-mediated <t>FLAG-DVL3</t> phosphorylation by CNH. (G) Schematic representation of HGK-induced phosphorylation of DVL3. The sites were identified by phospho proteomics. Different color represents relative enrichment of phosphorylation when compared to the control without ectopic HGK. APP: Amyloid precursor protein; CNH: Citron homology domain; Ctrl: control; DVL3: dishevelled segment polarity protein 3; GFP: green fluorescent protein; HA: hemagglutinin; p-Thr: phospho-threonine.
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CNH inhibits MAP4K-induced phosphorylation of DVL3. (A) Co-immunoprecipitation results showing the interaction of CNH with DVL3. (B) Co-immunoprecipitation results showing the interaction of DVL3 with HGK, MINK1, or TNIK. (C) The PDZ domain of DVL3 mediates its interaction with MINK1. DIX: homology region between DIshevelled and aXin; PDZ: homology region shared by PSD95, Dlg1, and Zo-1; DEP: shared homology region between Dishevelled, Egl-10, and Pleckstrin domain. (D) Mobility shift of DVL3 induced by wild-type but not kinase-dead (K54R) MAP4Ks. The migration front of the indicated protein bands is marked by a red line. (E) Western blots showing MAP4K-induced threonine phosphorylation of DLV3, which could be largely abolished after treatment with lambda protein phosphatase (λPP). p-Thr, antibody specific for phosphorylated threonine. (F) Phos-tag SDS-PAGE and western blotting to show suppression of HGK-mediated <t>FLAG-DVL3</t> phosphorylation by CNH. (G) Schematic representation of HGK-induced phosphorylation of DVL3. The sites were identified by phospho proteomics. Different color represents relative enrichment of phosphorylation when compared to the control without ectopic HGK. APP: Amyloid precursor protein; CNH: Citron homology domain; Ctrl: control; DVL3: dishevelled segment polarity protein 3; GFP: green fluorescent protein; HA: hemagglutinin; p-Thr: phospho-threonine.
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anti dykddddk g1 affinity resin  (GenScript corporation)
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CNH inhibits MAP4K-induced phosphorylation of DVL3. (A) Co-immunoprecipitation results showing the interaction of CNH with DVL3. (B) Co-immunoprecipitation results showing the interaction of DVL3 with HGK, MINK1, or TNIK. (C) The PDZ domain of DVL3 mediates its interaction with MINK1. DIX: homology region between DIshevelled and aXin; PDZ: homology region shared by PSD95, Dlg1, and Zo-1; DEP: shared homology region between Dishevelled, Egl-10, and Pleckstrin domain. (D) Mobility shift of DVL3 induced by wild-type but not kinase-dead (K54R) MAP4Ks. The migration front of the indicated protein bands is marked by a red line. (E) Western blots showing MAP4K-induced threonine phosphorylation of DLV3, which could be largely abolished after treatment with lambda protein phosphatase (λPP). p-Thr, antibody specific for phosphorylated threonine. (F) Phos-tag SDS-PAGE and western blotting to show suppression of HGK-mediated <t>FLAG-DVL3</t> phosphorylation by CNH. (G) Schematic representation of HGK-induced phosphorylation of DVL3. The sites were identified by phospho proteomics. Different color represents relative enrichment of phosphorylation when compared to the control without ectopic HGK. APP: Amyloid precursor protein; CNH: Citron homology domain; Ctrl: control; DVL3: dishevelled segment polarity protein 3; GFP: green fluorescent protein; HA: hemagglutinin; p-Thr: phospho-threonine.
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anti dykddddk  (TransGen biotech co)
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CNH inhibits MAP4K-induced phosphorylation of DVL3. (A) Co-immunoprecipitation results showing the interaction of CNH with DVL3. (B) Co-immunoprecipitation results showing the interaction of DVL3 with HGK, MINK1, or TNIK. (C) The PDZ domain of DVL3 mediates its interaction with MINK1. DIX: homology region between DIshevelled and aXin; PDZ: homology region shared by PSD95, Dlg1, and Zo-1; DEP: shared homology region between Dishevelled, Egl-10, and Pleckstrin domain. (D) Mobility shift of DVL3 induced by wild-type but not kinase-dead (K54R) MAP4Ks. The migration front of the indicated protein bands is marked by a red line. (E) Western blots showing MAP4K-induced threonine phosphorylation of DLV3, which could be largely abolished after treatment with lambda protein phosphatase (λPP). p-Thr, antibody specific for phosphorylated threonine. (F) Phos-tag SDS-PAGE and western blotting to show suppression of HGK-mediated <t>FLAG-DVL3</t> phosphorylation by CNH. (G) Schematic representation of HGK-induced phosphorylation of DVL3. The sites were identified by phospho proteomics. Different color represents relative enrichment of phosphorylation when compared to the control without ectopic HGK. APP: Amyloid precursor protein; CNH: Citron homology domain; Ctrl: control; DVL3: dishevelled segment polarity protein 3; GFP: green fluorescent protein; HA: hemagglutinin; p-Thr: phospho-threonine.
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pre equilibrated anti dykddddk tag antibody beads  (FUJIFILM)
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CNH inhibits MAP4K-induced phosphorylation of DVL3. (A) Co-immunoprecipitation results showing the interaction of CNH with DVL3. (B) Co-immunoprecipitation results showing the interaction of DVL3 with HGK, MINK1, or TNIK. (C) The PDZ domain of DVL3 mediates its interaction with MINK1. DIX: homology region between DIshevelled and aXin; PDZ: homology region shared by PSD95, Dlg1, and Zo-1; DEP: shared homology region between Dishevelled, Egl-10, and Pleckstrin domain. (D) Mobility shift of DVL3 induced by wild-type but not kinase-dead (K54R) MAP4Ks. The migration front of the indicated protein bands is marked by a red line. (E) Western blots showing MAP4K-induced threonine phosphorylation of DLV3, which could be largely abolished after treatment with lambda protein phosphatase (λPP). p-Thr, antibody specific for phosphorylated threonine. (F) Phos-tag SDS-PAGE and western blotting to show suppression of HGK-mediated <t>FLAG-DVL3</t> phosphorylation by CNH. (G) Schematic representation of HGK-induced phosphorylation of DVL3. The sites were identified by phospho proteomics. Different color represents relative enrichment of phosphorylation when compared to the control without ectopic HGK. APP: Amyloid precursor protein; CNH: Citron homology domain; Ctrl: control; DVL3: dishevelled segment polarity protein 3; GFP: green fluorescent protein; HA: hemagglutinin; p-Thr: phospho-threonine.
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apc anti dykddddk tag antibody  (Revvity)
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CNH inhibits MAP4K-induced phosphorylation of DVL3. (A) Co-immunoprecipitation results showing the interaction of CNH with DVL3. (B) Co-immunoprecipitation results showing the interaction of DVL3 with HGK, MINK1, or TNIK. (C) The PDZ domain of DVL3 mediates its interaction with MINK1. DIX: homology region between DIshevelled and aXin; PDZ: homology region shared by PSD95, Dlg1, and Zo-1; DEP: shared homology region between Dishevelled, Egl-10, and Pleckstrin domain. (D) Mobility shift of DVL3 induced by wild-type but not kinase-dead (K54R) MAP4Ks. The migration front of the indicated protein bands is marked by a red line. (E) Western blots showing MAP4K-induced threonine phosphorylation of DLV3, which could be largely abolished after treatment with lambda protein phosphatase (λPP). p-Thr, antibody specific for phosphorylated threonine. (F) Phos-tag SDS-PAGE and western blotting to show suppression of HGK-mediated <t>FLAG-DVL3</t> phosphorylation by CNH. (G) Schematic representation of HGK-induced phosphorylation of DVL3. The sites were identified by phospho proteomics. Different color represents relative enrichment of phosphorylation when compared to the control without ectopic HGK. APP: Amyloid precursor protein; CNH: Citron homology domain; Ctrl: control; DVL3: dishevelled segment polarity protein 3; GFP: green fluorescent protein; HA: hemagglutinin; p-Thr: phospho-threonine.
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CNH inhibits MAP4K-induced phosphorylation of DVL3. (A) Co-immunoprecipitation results showing the interaction of CNH with DVL3. (B) Co-immunoprecipitation results showing the interaction of DVL3 with HGK, MINK1, or TNIK. (C) The PDZ domain of DVL3 mediates its interaction with MINK1. DIX: homology region between DIshevelled and aXin; PDZ: homology region shared by PSD95, Dlg1, and Zo-1; DEP: shared homology region between Dishevelled, Egl-10, and Pleckstrin domain. (D) Mobility shift of DVL3 induced by wild-type but not kinase-dead (K54R) MAP4Ks. The migration front of the indicated protein bands is marked by a red line. (E) Western blots showing MAP4K-induced threonine phosphorylation of DLV3, which could be largely abolished after treatment with lambda protein phosphatase (λPP). p-Thr, antibody specific for phosphorylated threonine. (F) Phos-tag SDS-PAGE and western blotting to show suppression of HGK-mediated FLAG-DVL3 phosphorylation by CNH. (G) Schematic representation of HGK-induced phosphorylation of DVL3. The sites were identified by phospho proteomics. Different color represents relative enrichment of phosphorylation when compared to the control without ectopic HGK. APP: Amyloid precursor protein; CNH: Citron homology domain; Ctrl: control; DVL3: dishevelled segment polarity protein 3; GFP: green fluorescent protein; HA: hemagglutinin; p-Thr: phospho-threonine.

Journal: Neural Regeneration Research

Article Title: The Citron homology domain of MAP4Ks improves outcomes of traumatic brain injury

doi: 10.4103/NRR.NRR-D-24-00113

Figure Lengend Snippet: CNH inhibits MAP4K-induced phosphorylation of DVL3. (A) Co-immunoprecipitation results showing the interaction of CNH with DVL3. (B) Co-immunoprecipitation results showing the interaction of DVL3 with HGK, MINK1, or TNIK. (C) The PDZ domain of DVL3 mediates its interaction with MINK1. DIX: homology region between DIshevelled and aXin; PDZ: homology region shared by PSD95, Dlg1, and Zo-1; DEP: shared homology region between Dishevelled, Egl-10, and Pleckstrin domain. (D) Mobility shift of DVL3 induced by wild-type but not kinase-dead (K54R) MAP4Ks. The migration front of the indicated protein bands is marked by a red line. (E) Western blots showing MAP4K-induced threonine phosphorylation of DLV3, which could be largely abolished after treatment with lambda protein phosphatase (λPP). p-Thr, antibody specific for phosphorylated threonine. (F) Phos-tag SDS-PAGE and western blotting to show suppression of HGK-mediated FLAG-DVL3 phosphorylation by CNH. (G) Schematic representation of HGK-induced phosphorylation of DVL3. The sites were identified by phospho proteomics. Different color represents relative enrichment of phosphorylation when compared to the control without ectopic HGK. APP: Amyloid precursor protein; CNH: Citron homology domain; Ctrl: control; DVL3: dishevelled segment polarity protein 3; GFP: green fluorescent protein; HA: hemagglutinin; p-Thr: phospho-threonine.

Article Snippet: The following primary antibodies were used for western blot: FLAG (1:5000, Cat# 20543-1-AP, Proteintech, Rosemont, IL, USA), HA (1:5000, Cat# MMS-101P, Biolegend), phospho-threonine (p-Thr; 1:1000, Cat# 9386, Cell Signaling Technology, Danvers, MA, USA), actin beta (ACTB; 1:10000, Cat# HRP-66009, Proteintech), catenin beta 1 (CTNB1; 1:3000, Cat# 9386, Cell Signaling Technology), p-JNK (1:2000, Cat# 9251, Cell Signaling Technology), JNK (1:3000, Cat# A5005, Selleckchem, Houston, TX, USA).

Techniques: Immunoprecipitation, Mobility Shift, Migration, Western Blot, SDS Page, Control