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Int. J. Mol. Sci. 2017, 18(12), 2601; doi:10.3390/ijms18122601

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

1
College of Pharmacy, Sunchon National University, 255 Jungang-ro, Sunchon, Jeonnam 57922, Korea
2
Medical Research Center for Gene Regulation, Brain Korea 21 Project, Chonnam National University Medical School, 160 Baekseo-ro, Dong-gu, Gwangju 61469, Korea
3
Korea Basic Science Institute, Gwangju Center, 77 Yongbong-ro, Buk-gu, Gwangju 61186, Korea
4
Department of Dental Pharmacology, School of Dentistry and Institute of Oral Bioscience, BK21 Plus, Chonbuk National University, 567 Baekje-daero, Jeonju, Jeonbuk 54896, Korea
These authors contributed equally to this work.
*
Authors to whom correspondence should be addressed.
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 2017)
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Abstract

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
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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.

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