Systems Proteomics View of the Endogenous Human Claudin Protein Family

• 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
• Journal Title: Journal of Proteome Research
• Volume: Volume 15, Number 2
• Publisher: American Chemical Society | 2016-02-05, Pages 339-359
• Type of Work: Article | Post-print: After Peer Review
• Publisher DOI: http://doi.org/10.1021/acs.jproteome.5b00769
• Subjects: Biology, Molecular; Chemistry, Biochemistry; Biology, Cell
• Keywords: Science & Technology; Life Sciences & Biomedicine; Biochemical Research Methods; Biochemistry & Molecular Biology; Membrane protein complexes; cell-contact signaling systems proteomics; membrane proteomics; targeted proteomics; top-down proteomics; chemical proteomics; HEPATITIS-C-VIRUS; BLOOD-BRAIN-BARRIER; TIGHT JUNCTION PROTEINS; TOP-DOWN PROTEOMICS; CLOSTRIDIUM-PERFRINGENS ENTEROTOXIN; INTEGRAL MEMBRANE-PROTEINS; TANDEM MASS-SPECTROMETRY; EMBRYONIC STEM-CELLS; E3 UBIQUITIN LIGASE; LUNG-CANCER CELLS

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.