Figures
In Fig 1, there were two instances of Fig 1B, whereas the figure legend referred to the presence of a Fig 1C. In Fig 2, the authors provide the correct HA-APPY panel in Fig 2B. The published panel resulted from an inadvertent duplication of another gel, part of which correctly appears in lanes 2–4 of the HA-APPY panel in Fig 3A. In Fig 6, the authors provide the correct APP-mGFP and CTF-mGFP panels in Fig 6B. The published panel resulted from an inadvertent duplication of the middle panels in Fig 6A. An error in labeling the top and middle panels of Fig 6A has been corrected. The original underlying quantitative data for this article were not included with the published article, but are now presented with this notice in S2 File.
A. Cells expressing APPV5 or APPV5 plus HA-APPY were subjected to co-immunoprecipitation assays to detect APPV5/HA-APPY interaction or APP-dimerization. APPV5 was immunoprecipitated with an anti-V5 antibody. Immunoprecipitates were probed with an anti-HA antibody to detect pull-down of HA-APPY. Subsequently the immunoprecipitates were subjected to mABE assay to detect palAPPV5/HA-APPY interaction (or palAPP-dimerization). PalAPPV5 pulled down both palAPPV5 (Mwt ~102 kD) and palHA-APPY (Mwt ~150 kD) from cells expressing APPV5 plus HA-APPY but not from cells expressing only APPV5. B. TotAPP-dimers (APPV5/HA-APPY) only form in cells expressing both APPV5 and HA-APPY. C. Quantitation of palAPP-dimers (palAPPV5/palHA-APPY) versus totAPP-dimers (APPV5/HA-APPY). Error bars show the s.e.m. (**p<0.01). D. palAPP dimerizes is cis-orientiation. Cells expressing HA-APPY and cells expressing mycAPP were co-cultured in absence or presence of 1mM cell-impermeable cross-linker DTSSP. Cell extracts were subjected to a pull-down assay, using an anti-HA antibody to immunoprecipitate HA-APPY. To test for APP-dimerization, the precipitates were probed with an anti-myc antibody (panel b, co-culture). Cells co-expressing HA-APPY and mycAPP were also subjected to a co-IP assay using the anti-HA antibody to pull-down mycAPP with HA-APPY.(panel b, co-expression). To detect palAPP-dimerization, the immunoprecipitates were also subjected to mABE assay to detect co-IP of palHA-APPY with pal-mycAPP (panel a). The experiment is a representative of three independent experiments.
A. Schematic representation of the Cys to Ser mutants of APP used for the following co-immunoprecipitation assays. B. Co-immunoprecipitation assay in cells co-expressing APPV5 and HA-APPY and its mutants containing indicated Cys to Ser substitution. HA-APPY pulls down APPV5, indicating APP-APP dimerization. APP(C133S) and APP(C158S) show 2 fold increase in dimerization, while APP(C186S) and APP(C187S) fail to dimerize. APP(C186S) and APP(C187S) generated trace amounts of palmitoylation-independent dimers (* and **). C. ABE assay of cells overexpressing indicated APP mutants show 2 fold increased palmitoylation of APP(C133S) and APP(C158S), where as APP(C186S) and APP(C187S) were defective in palmitoylation.
A. Naïve CHO cells co-expressing APPV5 and APPHA were subjected to a co-IP assay in presence of DMSO (0 μg/ml) or increasing concentrations of cerulenin (25, 50 and 100 μg/ml). flAPPHA (APPHA) pulled down fl- as well as the C-terminal fragments of APPV5 (APPV5 and CTFV5, respectively) in DMSO-treated (0 μg/ml cerulenin) cells. In presence of cerulenin, co-IP of flAPPV5 (APPV5) with flAPPHA (APPHA) decreased in a dose-dependent manner. Little or no co-IP of flAPP observed upon treatment with100 μg/ml cerulenin. In contrast, cerulenin had no effect on CTFV5 pull-down even at the highest concentration (100 μg/ml). Cerulenin reduced palAPPHA levels in a dose-dependent manner (ABE assay) reaching complete inhibition at 100 μg/ml concentration. B. co-IP assay using an antibody specific for mGFP (anti-mGFP) to pull-down full-length (fl) APPmGFP with APPmCherry from differentiated neuronal cells (RenVM) co-expressing APPmGFP+APPmCherry. Anti-mGFP also pulled-down CTFmCherry with CTFmGFP. Cerulenin (25 μg/ml) treatment of the cells prior to co-IP assay dramatically decreased flAPPmGFP-flAPPmCherry interaction, but not that of CTFmGFP-CTFmCherry.
With this correction of this article [1], the authors provide updated versions of Fig 1, Fig 2, and Fig 6; original uncropped underlying blots for the figures of concern (S1 File); and the original underlying quantitative data for this article (S2 File).
The authors apologize for the errors in the published article.
Supporting information
S1 File. Raw Western blot data for Figs 2, 3, and 6.
https://doi.org/10.1371/journal.pone.0299972.s001
(PPTX)
S2 File. Quantitative data for Figs 1, 3, 4, and 5.
https://doi.org/10.1371/journal.pone.0299972.s002
(PPTX)
Reference
- 1. Bhattacharyya R, Fenn RH, Barren C, Tanzi RE, Kovacs DM (2016) Palmitoylated APP Forms Dimers, Cleaved by BACE1. PLoS ONE 11(11): e0166400. https://doi.org/10.1371/journal.pone.0166400 pmid:27875558
Citation: Bhattacharyya R, Fenn RH, Barren C, Tanzi RE, Kovacs DM (2024) Correction: Palmitoylated APP Forms Dimers, Cleaved by BACE1. PLoS ONE 19(2): e0299972. https://doi.org/10.1371/journal.pone.0299972
Published: February 29, 2024
Copyright: © 2024 Bhattacharyya et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.