A pseudosymmetric cell adhesion regulatory domain in the β7 tail of the integrin α4β7 that interacts with focal adhesion kinase and src Krissansen, Geoffrey W., Singh, Jaison, Kanwar, Rupinder K., Chan, Yih-Chih, Leung, Euphemia, Lehnert, Klaus B., Kanwar, Jagat R. and Yang, Yi 2006, A pseudosymmetric cell adhesion regulatory domain in the β7 tail of the integrin α4β7 that interacts with focal adhesion kinase and src, European journal of immunology, vol. 36, no. 8, pp. 2203-2214, doi: 10.1002/eji.200535324. Attached Files Name Description MIMEType Size Downloads Title A pseudosymmetric cell adhesion regulatory domain in the β7 tail of the integrin α4β7 that interacts with focal adhesion kinase and src Author(s) Krissansen, Geoffrey W. Singh, Jaison Kanwar, Rupinder K. Chan, Yih-Chih Leung, Euphemia Lehnert, Klaus B. Kanwar, Jagat R. orcid.org/0000-0003-3728-9568 Yang, Yi Journal name European journal of immunology Volume number 36 Issue number 8 Start page 2203 End page 2214 Publisher Wiley - V C H Verlag GmbH & Co. KGaA Place of publication Weinheim, Germany Publication date 2006-08 ISSN 0014-2980 1521-4141 Keyword(s) β7 integrin cell adhesion regulatory domain kinases signal transduction T cells Summary The β7 integrins α4β7 and Eβ7 play key roles in forming the gut-associated lymphoid tissue, and contribute to chronic inflammation. The α4β7 integrin-mediated adhesion of activated lymphocytes is largely due to a transient increase in avidity from ligand-induced clustering of α4β7 at the cell-surface. Here, we report that L and D enantiomers of a cell-permeable peptide YDRREY encompassing residues 735-740 of the cytoplasmic tail of the β7 subunit inhibit the adhesion of T cells to β7 integrin ligands. The YDRREY peptide abrogated mucosal addressin cell adhesion molecule-1-induced clustering of α4β7 on the surface of activated T cells. A mutated form of the YDRREY peptide carrying either single or double conservative mutations at Tyr735Phe and Tyr740Phe was unable to inhibit T cell adhesion, suggesting that both tandem tyrosines are critical for activity. The YDRREY peptide was bound and phosphorylated by focal adhesion kinase and src, which may serve to sequester cytoskeletal proteins to the cytoplasmic domain of 4β7. The quasi-palindromic sequence YDRREY within the β7 cytoplasmic tail constitutes a cell adhesion regulatory domain that modulates the interaction of β7-expressing leukocytes with their endothelial and epithelial ligands. Cell-permeable peptidomimetics based on this motif have utility as anti-inflammatory reagents for the treatment of chronic inflammatory disease. Language eng DOI 10.1002/eji.200535324 Field of Research 060199 Biochemistry and Cell Biology not elsewhere classified HERDC Research category C1.1 Refereed article in a scholarly journal HERDC collection year 2008 Copyright notice ©2006, WILEY-VCH Verlag GmbH & Co Free to Read? Yes Persistent URL http://hdl.handle.net/10536/DRO/DU:30019771 Document type: Journal Article Collections: Faculty of Science, Engineering and Built Environment Institute of Biotechnology Open Access Collection Related Links Link Description Link to full-text (open access)   Connect to published version (restricted access) Go to link with your DU access privileges     Unless expressly stated otherwise, the copyright for items in DRO is owned by the author, with all rights reserved. Every reasonable effort has been made to ensure that permission has been obtained for items included in DRO. If you believe that your rights have been infringed by this repository, please contact drosupport@deakin.edu.au. Versions Version Filter Type Tue, 22 Sep 2009, 14:56:01 EST Tue, 22 Sep 2009, 14:58:38 EST Tue, 22 Sep 2009, 15:45:32 EST Thu, 17 Jun 2010, 12:42:09 EST Mon, 16 Jun 2014, 13:03:15 EST Thu, 01 Oct 2020, 17:36:02 EST Filtered Full Citation counts:   Cited 13 times in TR Web of Science Cited 14 times in Scopus Search Google Scholar Access Statistics: 830 Abstract Views, 0 File Downloads  -  Detailed Statistics Created: Tue, 22 Sep 2009, 14:55:58 EST by Lorraine Driscoll

Every reasonable effort has been made to ensure that permission has been obtained for items included in DRO. If you believe that your rights have been infringed by this repository, please contact drosupport@deakin.edu.au.