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Author Notes:

Corresponding Author, fei.liu@mq.edu.au. Tel: (61)-2-9850-8312. Fax: (61)-2-9850-8313.

The authors declare no competing financial interest.

Subjects:

Research Funding:

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:

  • 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

Systems Proteomics View of the Endogenous Human Claudin Protein Family

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Journal Title:

Journal of Proteome Research

Volume:

Volume 15, Number 2

Publisher:

, Pages 339-359

Type of Work:

Article | Post-print: After Peer Review

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.

Copyright information:

© 2015 American Chemical Society.

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