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. 2024 Feb 7;15:1148. doi: 10.1038/s41467-024-45324-w

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© The Author(s) 2024

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 3 — a (left) Global phosphoproteomic profiling of EV vs. FUT4-overexpressing (OE) melanoma cells treated with 10 μM ARi for 48 h. Volcano plots showing phosphopeptides identified by LC-MS/MS to be ≥2-fold-change (FC) reduced by ARi (center left) that are or are not rescued by FUT4-OE (center right). p-values are calculated by two-sided Student’s t-test. DAVID pathway analysis identifying the enrichment of cell division-related signaling as AR-dependent, FUT4-independent (upper right) vs. cell adhesion-related signaling as AR- and FUT4-dependent (lower right). In DAVID, one-sided Fisher’s Exact test is adopted to measure the gene-enrichment in annotation terms. b Ingenuity Pathway Analysis (IPA) highlighting AR-FUT4-regulated protein signatures are predominantly enriched in adherens junction (AJ) signaling. p-values are calculated by one-sided Fisher’s Exact test. c Schematic diagram of AJ signaling between 2 adjacent cells (adapted from a Qiagen IPA-generated schematic). Red circles denote hits from our phosphoproteomic profiles. d In situ proximity ligation assay (PLA) for N-cadherin and catenin proteins in EV/FUT4-OE WM793 cells. N-cadherin/β-catenin PLA (upper): EV, n = 10 fields; FUT4-OE, n = 8 fields and N-cadherin/δ1-catenin PLA (lower): n = 7 fields examined over 1 independent experiment. Two other independent experiments in Source Data. Scale bar = 50 μm. e (upper) PLA and (lower) co-immunoprecipitation (co-IP) analyses evaluating the interaction between N-cadherin and β-catenin proteins in shNT/shFUT4 WM793 cells. PLA: shNT, n = 7 fields; shFUT4, n = 9 fields examined over 1 independent experiment. Two other independent experiments in Source Data. Scale bar=50μm. Co-IP: n = 4 biologically independent samples. Uncropped blots in Source Data. f PLA staining for N-cadherin and catenin proteins in parental WM793 cells treated ± 10 μM ARi for 48 h. N-cadherin/β-catenin PLA (upper): CTL, n = 11 fields; ARi, n = 8 fields and N-cadherin/δ1-catenin PLA (lower): n = 10 fields examined over 1 independent experiment. Two other independent experiments in Source Data. Scale bar = 50 μm. g Working model of AR-FUT4 axis in disrupting AJs to promote melanoma invasiveness (the schematic was created using BioRender). For d–f, data are presented as mean values ± SEM and p-values are calculated by two-sided Student’s t-test. Source data are provided as a Source Data file.