Next Article in Journal
Sulfur-Mediated-Alleviation of Aluminum-Toxicity in Citrus grandis Seedlings
Next Article in Special Issue
Receptor-Like Kinase LYK9 in Pisum sativum L. Is the CERK1-Like Receptor that Controls Both Plant Immunity and AM Symbiosis Development
Previous Article in Journal
Rapid Non-Enzymatic Glycation of the Insulin Receptor under Hyperglycemic Conditions Inhibits Insulin Binding In Vitro: Implications for Insulin Resistance
Previous Article in Special Issue
Conditioned Medium from Malignant Breast Cancer Cells Induces an EMT-Like Phenotype and an Altered N-Glycan Profile in Normal Epithelial MCF10A Cells
Open AccessArticle

Glycoprotein 90K Promotes E-Cadherin Degradation in a Cell Density-Dependent Manner via Dissociation of E-Cadherin–p120-Catenin Complex

College of Pharmacy, Sunchon National University, 255 Jungang-ro, Sunchon, Jeonnam 57922, Korea
Medical Research Center for Gene Regulation, Brain Korea 21 Project, Chonnam National University Medical School, 160 Baekseo-ro, Dong-gu, Gwangju 61469, Korea
Korea Basic Science Institute, Gwangju Center, 77 Yongbong-ro, Buk-gu, Gwangju 61186, Korea
Department of Dental Pharmacology, School of Dentistry and Institute of Oral Bioscience, BK21 Plus, Chonbuk National University, 567 Baekje-daero, Jeonju, Jeonbuk 54896, Korea
Authors to whom correspondence should be addressed.
These authors contributed equally to this work.
Int. J. Mol. Sci. 2017, 18(12), 2601;
Received: 14 October 2017 / Revised: 23 November 2017 / Accepted: 28 November 2017 / Published: 2 December 2017
(This article belongs to the Special Issue Glycan–Receptor Interaction 2018)
Glycoprotein 90K (also known as LGALS3BP or Mac-2BP) is a tumor-associated protein, and high 90K levels are associated with poor prognosis in some cancers. To clarify the role of 90K as an indicator for poor prognosis and metastasis in epithelial cancers, the present study investigated the effect of 90K on an adherens junctional protein, E-cadherin, which is frequently absent or downregulated in human epithelial cancers. Treatment of certain cancer cells with 90K significantly reduced E-cadherin levels in a cell-population-dependent manner, and these cells showed decreases in cell adhesion and increases in invasive cell motility. Mechanistically, 90K-induced E-cadherin downregulation occurred via ubiquitination-mediated proteasomal degradation. 90K interacted with the E-cadherin–p120-catenin complex and induced its dissociation, altering the phosphorylation status of p120-catenin, whereas it did not associate with β-catenin. In subconfluent cells, 90K decreased membrane-localized p120-catenin and the membrane fraction of the p120-catenin. Particularly, 90K-induced E-cadherin downregulation was diminished in p120-catenin knocked-down cells. Taken together, 90K upregulation promotes the dissociation of the E-cadherin–p120-catenin complex, leading to E-cadherin proteasomal degradation, and thereby destabilizing adherens junctions in less confluent tumor cells. Our results provide a potential mechanism to explain the poor prognosis of cancer patients with high serum 90K levels. View Full-Text
Keywords: 90K glycoprotein; LGALS3BP; Mac-2BP; E-cadherin; p120-catenin; adherens junction 90K glycoprotein; LGALS3BP; Mac-2BP; E-cadherin; p120-catenin; adherens junction
Show Figures

Figure 1

MDPI and ACS Style

Park, S.-Y.; Yoon, S.; Sun, E.G.; Zhou, R.; Bae, J.A.; Seo, Y.-W.; Chae, J.-I.; Paik, M.-J.; Ha, H.-H.; Kim, H.; Kim, K.K. Glycoprotein 90K Promotes E-Cadherin Degradation in a Cell Density-Dependent Manner via Dissociation of E-Cadherin–p120-Catenin Complex. Int. J. Mol. Sci. 2017, 18, 2601.

Show more citation formats Show less citations formats
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

Back to TopTop