Add to Quick Collection
Please use this identifier to cite or link to this item: http://hdl.handle.net/1959.14/1192167
1017 Visitors
1115 Hits
0 Downloads
- Title
- Systems proteomics view of the endogenous human claudin protein family
- Related
- Journal of proteome research, Vol. 15, Issue 2, (2016), p.339-359
- Funding Body
- ARC
- Funding Body
- NHMRC
- Grant URL
- http://purl.org/au-research/grants/arc/LIEF150100161
- Grant URL
- http://purl.org/au-research/grants/nhmrc/1010303
- DOI
- 10.1021/acs.jproteome.5b00769
- Publisher
- American Chemical Society
- Date
- 2016
- Author/Creator
- Liu, Fei
- Author/Creator
- Koval, Michael
- Author/Creator
- Kelleher, Neil L
- Author/Creator
- Baker, Mark S
- Author/Creator
- Ranganathan, Shoba
- Author/Creator
- Fanayan, Susan
- Author/Creator
- Hancock, William S
- Author/Creator
- Lundberg, Emma K
- Author/Creator
- Beavis, Ronald C
- Author/Creator
- Lane, Lydie
- Author/Creator
- Duek, Paula
- Author/Creator
- McQuade, Leon
- Description
- 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.
- Description
- 21 page(s)
- Subject Keyword
- membrane protein complexes
- Subject Keyword
- cell-contact signaling
- Subject Keyword
- systems proteomics
- Subject Keyword
- membrane proteomics
- Subject Keyword
- targeted proteomics
- Subject Keyword
- top-down proteomics
- Subject Keyword
- chemical proteomics
- Resource Type
- journal article
- Organisation
- Macquarie University. Department of Chemistry and Biomolecular Sciences
- Organisation
- Macquarie University. Department of Biological Sciences
- Organisation
- Macquarie University. Australian Proteome Analysis Facility (APAF)
- Identifier
- http://hdl.handle.net/1959.14/1192167
- Identifier
- mq:61144
- Identifier
- ISSN:1535-3893
- Identifier
- mq-rm-2014006471
- Identifier
- mq_res-se-533670
- Language
- eng
- Reviewed
Macquarie University ResearchOnline
