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Image Search Results
Journal: Journal of Biological Chemistry
Article Title: Multisite NHERF1 phosphorylation controls GRK6A regulation of hormone-sensitive phosphate transport
doi: 10.1016/j.jbc.2021.100473
Figure Lengend Snippet: Figure 2. GRK6A binds PDZ1–NHERF1 under resting conditions. A, representative immunoblot of NHERF1:GRK6A coIP. HA-GRK6A was cotransfected with either empty vector or the indicated FLAG–NHERF1 construct into OKH cells. WT-NHERF1 coimmunoprecipitates with GRK6A, as does N1P2–GAGA– NHERF1 (PDZ1 intact). N1P1–GAGA (PDZ2 intact) and N1P1P2–GAGA/GAGA (both PDZ domains are modified) do not interact with NHERF1. B, NHERF1 coIP with GRK6A was quantified in transfected OKH cells and normalized to WT-NHERF1 (100%). N1P2 interacts with GRK6A to a similar extent to WT-NHERF1. Disruption of PDZ1 (N1P1–GAGA, N1P1P2–GAGA/GAGA) eliminated binding of GRK6A. Results report the mean ± SD (n = 3; ****p < 0.0001, ANOVA). coIP, coimmunoprecipitation; GRK6A, G protein–coupled receptor kinase 6A; NHERF1, Na+/H+ exchange regulatory factor-1.
Article Snippet: Chemically competent E. coli BL21 ΔSerB (
Techniques: Western Blot, Plasmid Preparation, Construct, Transfection, Disruption, Binding Assay
Journal: Journal of Biological Chemistry
Article Title: Multisite NHERF1 phosphorylation controls GRK6A regulation of hormone-sensitive phosphate transport
doi: 10.1016/j.jbc.2021.100473
Figure Lengend Snippet: Figure 7. General scheme represents the order of events along NHERF1-dependent PTH-sensitive phosphate uptake. NHERF1 PDZ1 binds NPT2A through the C-terminal (-TRL) motif and that keeps NPT2A at the apical membrane. PTH-induced phosphorylation promotes phosphorylation of Ser162 by PKCα. GRK6A binds pSer162−PDZ2 through the C-terminal (-TRL) motif and phosphorylates Ser290. NPT2A dissociates from NHERF1 and internalizes. GRK6A, G protein–coupled receptor kinase 6A; NHERF1, Na+/H+ exchange regulatory factor-1; PTH, parathyroid hormone.
Article Snippet: Chemically competent E. coli BL21 ΔSerB (
Techniques: Membrane, Phospho-proteomics