Pan-claudin family interactome analysis reveals shared and specific interactions.
Autor: | Suarez-Artiles L; Max-Delbrück Center, Berlin, Germany., Breiderhoff T; Division of Gastroenterology, Nephrology and Metabolic Diseases, Department of Pediatrics, Charité-Universitätsmedizin Berlin, Berlin, Germany., Girardello R; Proteomics of Cellular Signaling, Luxembourg Institute of Health, Strassen, Luxembourg., Gonschior H; Leibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP), Berlin, Germany., Rodius S; Proteomics of Cellular Signaling, Luxembourg Institute of Health, Strassen, Luxembourg., Lesur A; Proteomics of Cellular Signaling, Luxembourg Institute of Health, Strassen, Luxembourg., Reimer U; JPT GmbH, Berlin, Germany., Ramberger E; Max-Delbrück Center, Berlin, Germany; German Cancer Consortium (DKTK), Partner Site Berlin, Germany; German Cancer Research Center (DKFZ), Heidelberg, Germany; Department of Internal Medicine with Focus on Hematology, Oncology and Tumor Immunology,Charité-Universitätsmedizin Berlin, Berlin, Germany., Perez-Hernandez D; Proteomics of Cellular Signaling, Luxembourg Institute of Health, Strassen, Luxembourg., Müller D; Division of Gastroenterology, Nephrology and Metabolic Diseases, Department of Pediatrics, Charité-Universitätsmedizin Berlin, Berlin, Germany. Electronic address: dominik.mueller@charite.de., Mertins P; Max-Delbrück Center, Berlin, Germany; Berlin Institute of Health (BIH), Berlin, Germany; German Cancer Consortium (DKTK), Partner Site Berlin, Germany; German Centre for Cardiovascular Research (DZHK), Berlin, Germany. Electronic address: philipp.mertins@mdc-berlin.de., Dittmar G; Proteomics of Cellular Signaling, Luxembourg Institute of Health, Strassen, Luxembourg; Department of Life Sciences and Medicine, University of Luxembourg, Campus Belval, Luxembourg. Electronic address: gunnar.dittmar@lih.lu. |
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Jazyk: | angličtina |
Zdroj: | Cell reports [Cell Rep] 2022 Nov 08; Vol. 41 (6), pp. 111588. |
DOI: | 10.1016/j.celrep.2022.111588 |
Abstrakt: | Claudins are a family of transmembrane proteins expressed in epithelial tissues and are the major components of tight junctions (TJs), which define barrier properties in epithelia and maintain cell polarity. How claudins regulate the formation of TJs and which functions they exert outside of them is not entirely understood. Although the long and unstructured C-terminal tail is essential for regulation, it is unclear how it is involved in these functions beyond interacting with TJ-associated proteins such as TJ protein ZO-1 (TJP1). Here, we present an interactome study of the pan-claudin family in Madin-Darby canine kidney (MDCK)-C7 cells by combining two complementary mass spectrometry-based pull-down techniques creating an interaction landscape of the entire claudin family. The interaction partners of the claudins' C termini reveal their possible implications in localized biological processes in epithelial cells and their regulation by post-translational modifications (PTMs). Competing Interests: Declaration of interests The authors declare no competing interests. (Copyright © 2022 The Authors. Published by Elsevier Inc. All rights reserved.) |
Databáze: | MEDLINE |
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