In the article entitled “Evidence that Intestinal Intraepithelial Lymphocytes Are Activated Cytotoxic T Cells in Celiac Disease but Not in Giardiasis” (Volume 148, pages 1351 to 1357 in the May 1996 issue of The American Journal of Pathology), the fifth author’s name was incorrect. The correct name is J. Alain Kummer.
In the article entitled, “Ezrin-Radixin-Moesin-Binding Phosphoprotein (EBP50), an Estrogen-Inducible Scaffold Protein, Contributes to Biliary Epithelial Cell Proliferation” (Volume 174, pages 869 to 880 of the March 2009 issue), the footnote mistakenly stated that supplemental material was available online; there is no supplemental data for this article. In addition, the authors noted an error in panel order in Figure 1E. The corrected figure (with legend) appears below:
In the article entitled, “Salmonella Effector AvrA Regulation of Colonic Epithelial Cell Inflammation by Deubiquitination” (Volume 171, pages 882 to 89 of the September 2007 issue), there was an error in panel order in Figure 4C and D. The corrected figure (with legend) appears below.
Figure 1.
Normal hepatobiliary expression of EBP50 and binding partners. Detection of EBP50, ezrin, and CFTR in normal human liver (L), hepatocytes (H), intrahepatic bile ducts (BDs), and gallbladder epithelial cells (G) by conventional RT-PCR (representative of preparations from three patients) (A) and by qRT-PCR (B). Results of qRT-PCR are expressed as mRNA levels normalized to 18S rRNA and relative to the mean bile duct value (means ± SEM of three preparations; *P < 0.05 versus bile ducts). Immunostaining of normal human liver cryosections for EBP50 (C, red), which is detected in the canalicular domain (left and middle, arrowheads), in juxtacanalicular vesicles (left, arrow) in hepatocytes, and in the apical domain of bile ducts (middle, arrow) and of gallbladder epithelial cells (right); ezrin, detected in the apical domain of bile ducts (D); EBP50 (red, arrow) and CFTR (green, arrow), which are shown to co-localize (yellow, arrow) in the apical domain of bile ducts by double staining and confocal microscopy (E). An avidin-biotin immunofluorescence method was used except for ezrin, which was detected by alkaline phosphatase anti-alkaline phosphatase/Fast Red. L, Lumen.
Figure 4.
A: The Salmonella AvrA protein modulated β-catenin ubiquitination and activity. HeLa cells were incubated for 1 hour with PhoPc, AvrA−, or PhoPcAvrA−/AvrA+, washed, and incubated for the times indicated with the proteasome inhibitor MG262. Total cell lysates were analyzed for ubiquitinated β-catenin and β-actin (loading control) by immunoblot. Higher-molecular weight ubiquitinated β-catenin is indicated by arrows. Data shown are from a single experiment and are representative of three separate experiments. B: AvrA deubiquitinated ubiquitinated β-catenin. In the cell-free system, purified GST-AvrA or GST-C186A proteins were mixed with ubiquitinated β-catenin. The reaction was terminated in 60 minutes. The ubiquitinated forms of β-catenin were detected by immunoblot using anti-β-catenin antibody. The total amount of AvrA or C186A in each reaction was shown by immunoblot using anti-GST antibody. C: Location of β-catenin in HCT116 cells by immunofluorescence. Immunostaining of β-catenin in cells colonized with Salmonella PhoPc, AvrA−, or AvrA−/AvrA+. Cells were fixed, permeabilized, and stained with anti-β-catenin antibody, followed by A488 anti-mouse secondary antibody and 4,6-diamidino-2-phenylindole (DAPI). Arrows indicate cell nuclei. Images shown are from a single experiment and are representative of three separate repeats. D: AvrA regulates activation of the β-catenin-TCF signaling pathway. Cells were transiently transfected with a TCF-responsive luciferase reporter plasmid containing either a wild-type TCF-binding site (pGL3-OT) or a defective TCF binding site (pGL3-OF). Cells were then colonized with PhoPc or AvrA− for 30 minutes, washed, and incubated in medium for 6 hours. TCF-dependent transcription was measured by luciferase activity. Data are the means ± SD of a single experiment assayed in triplicate and are representative of three separate experiments.