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Image Search Results
Journal: FASEB journal : official publication of the Federation of American Societies for Experimental Biology
Article Title: LRRC8A anion channels modulate vascular reactivity via association with Myosin Phosphatase Rho Interacting Protein (MPRIP)
doi: 10.1096/fj.202300561R
Figure Lengend Snippet: A) Immunoprecipitation (IP) of endogenous LRRC8A from VSMCs confirms the presence of LRRC8A in the whole cell (WC) lysate and precipitated protein from WT but not LRRC8A KO cells. MPRIP is present in the WC lysate from both genotypes but is only pulled down in LRRC8A WT cells. B) Proximity Ligation Assay (PLA) signal from α-MPRIP/α-LRRC8A in WT VSMCs. Small white spots represent PLA signal, the larger spots are nuclei. Counts of spots/nucleus from multiple fields of confluent WT and LRRC8A KO VSMCs (20x). PLA spots were smaller and significantly less numerous in KO cells. The bottom image shows red PLA spots with green nuclei as a side-view of cells. C) Confocal images of HEK293T cells co-expressing LRRC8A-meGFP and MPRIP-mCherry. Note co-localization at the plasma membrane, particularly at ruffled borders but not in LRRC8A-containing intracellular vesicles. D) Sites of protein binding to MPRIP. The first Plextrin Homology (PH) domain (aa 44–152) binds actin. C-terminal coiled-coil domains mediate interaction with RhoA and MYPT1 (M). Below the map are the constructs utilized to determine the site of MPRIP binding to LRRC8A (8A) was localized to aa 389–545. Vertical grey lines represent specific cysteines that can be oxidized based upon the Oxymouse database (Cys103, 120, 235, 361, 506, 571, 723, 830). Susceptible cysteines are present in the binding regions for all 4 protein partners. E) Immunoprecipitation of MPRIP-DDK fragments by full length LRRC8A-Myc in HEK293T cells expressing these constructs. Arrows identify overexpressed proteins, or the site where they would be expected to run (see IP: α-Myc) in whole cell lysates (WCL, left) and in immunoprecipitated protein (IP, right). All C-terminal MPRIP deletion mutants associate with LRRC8A, but the C-terminal MPRIP fragment 879–1038 does not associate with LRRC8A. The 213–545 peptide associated with LRRC8A as did the region between 389 and 545 which contains PH2 (see IP: α-LRRC8A).
Article Snippet: A C-terminal tagged clone of
Techniques: Immunoprecipitation, Proximity Ligation Assay, Expressing, Clinical Proteomics, Membrane, Protein Binding, Construct, Binding Assay