Systems Proteomics View of the Endogenous Human Claudin Protein Family

• Type of Material: Article
• Authors: Fei Liu, Macquarie University; Michael Koval, Emory University; Shoba Ranganathan, Macquarie University; Susan Fanayan, Macquarie University; William S. Hancock, Macquarie University; Emma K. Lundberg, Royal Inst Technol KTH; Ronald C. Beavis, University of Manitoba; Lydie Lane, Royal Institute of Technology; Paula Duek, Swiss Institute of Bioinformatics; Leon McQuade, Macquarie University; Neil L. Kelleher, Northwestern University; Mark S. Baker, Macquarie University
• Language: English
• Date: 2016-02-05
• Publisher: American Chemical Society
• Publication Version: Author Accepted Manuscript (After Peer Review)
• Copyright Statement: © 2015 American Chemical Society.
• Final Published Version (URL): http://dx.doi.org/10.1021/acs.jproteome.5b00769
• Title of Journal or Parent Work: Journal of Proteome Research
• ISSN: 1535-3893
• Volume: 15
• Issue: 2
• Start Page: 339
• End Page: 359
• Grant/Funding Information: We thank the Australian Research Council (LIEF150100161 to F.L. and S.R.), the National Institute of Health (R01-HL116958 to M.K.), the National Health and Medical Research Council of Australia (NHMRC APP1010303 to M.S.B.), and the New South Wales Cancer Council (RG10-04 and RG08-16 to M.S.B.) for financial support.
• Keywords: CLOSTRIDIUM-PERFRINGENS ENTEROTOXIN; membrane proteomics; cell-contact signaling systems proteomics; TOP-DOWN PROTEOMICS; E3 UBIQUITIN LIGASE; targeted proteomics; chemical proteomics; Life Sciences & Biomedicine; EMBRYONIC STEM-CELLS; Biochemistry & Molecular Biology; TANDEM MASS-SPECTROMETRY; Biochemical Research Methods; HEPATITIS-C-VIRUS; TIGHT JUNCTION PROTEINS; BLOOD-BRAIN-BARRIER; top-down proteomics; INTEGRAL MEMBRANE-PROTEINS; LUNG-CANCER CELLS; Science & Technology; Membrane protein complexes
• Research Categories: Chemistry, Biochemistry; Biology, Cell; Biology, Molecular

Abstract

Claudins are the major transmembrane protein components of tight junctions in human endothelia and epithelia. Tissue-specific expression of claudin members suggests that this protein family is not only essential for sustaining the role of tight junctions in cell permeability control but also vital in organizing cell contact signaling by protein-protein interactions. How this protein family is collectively processed and regulated is key to understanding the role of junctional proteins in preserving cell identity and tissue integrity. The focus of this review is to first provide a brief overview of the functional context, on the basis of the extensive body of claudin biology research that has been thoroughly reviewed, for endogenous human claudin members and then ascertain existing and future proteomics techniques that may be applicable to systematically characterizing the chemical forms and interacting protein partners of this protein family in human. The ability to elucidate claudin-based signaling networks may provide new insight into cell development and differentiation programs that are crucial to tissue stability and manipulation.