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Blood, 15 April 2004, Vol. 103, No. 8, pp. 3013-3019. Prepublished online as a Blood First Edition Paper on December 18, 2003; DOI 10.1182/blood-2003-07-2201. This Article Full Text (PDF) Supplemental Video All Versions of this Article: 2003-07-2201v1 103/8/3013    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Kolesnikova, T. V Articles by Hemler, M. E Search for Related Content PubMed PubMed Citation Articles by Kolesnikova, T. V Articles by Hemler, M. E Social Bookmarking                   What's this? Submitted July 2, 2003 Accepted December 2, 2003 EWI-2 modulates lymphocyte integrin 41 functions Tatiana V Kolesnikova, Christopher S Stipp, Ravi M Rao, William S Lane, Francis W Luscinskas, and Martin E Hemler* CIA, Dana-Farber Cancer Institute, Boston, MA, USA Department of Pathology, Brigham and Women's Hospital, Boston, MA, USA Harvard Microchemistry Facility, Cambridge, MA, USA * Corresponding author; email: Martin_Hemler{at}DFCI.Harvard.EDU. The most prominent cell surface integrin 41 partner, a 70 kDa protein, was isolated from MOLT-4 T leukemia cells, using anti-41 integrin antibody-coated beads. By mass spectrometry, this protein was identified as EWI-2, a previously described cell surface partner for tetraspanin proteins CD9 and CD81. Wild type EWI-2 over-expression had no effect on MOLT-4 cell tethering and adhesion strengthening on the 4 ligand, VCAM-1, in shear flow assays. However, EWI-2 markedly impaired spreading and ruffling on VCAM-1. In contrast, a mutant EWI-2 molecule, with a different cytoplasmic tail, neither impaired cell spreading nor associated with 41 and CD81. The endogenous wild type EWI-2-CD81-41 complex was fully soluble, and highly specific as seen by the absence of other MOLT-4 cell surface proteins. Also it was relatively small in size (0.5-4x106), as estimated by size exclusion chromatography. Over-expression of EWI-2 in MOLT-4 cells caused reorganization of cell surface CD81, increased the extent of CD81-CD81, CD81-41, and 41-41 associations, and increased the apparent size of CD81-41 complexes. We suggest that EWI-2 dependent reorganization of 41-CD81 complexes on the cell surface is responsible for EWI-2 effects on integrin-dependent morphology and motility functions. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: S. Kettner, F. Kalthoff, P. Graf, E. Priller, F. Kricek, I. Lindley, and T. Schweighoffer EWI-2/CD316 Is an Inducible Receptor of HSPA8 on Human Dendritic Cells Mol. Cell. Biol., November 1, 2007; 27(21): 7718 - 7726. [Abstract] [Full Text] [PDF] O. V. Kovalenko, X. H. Yang, and M. E. Hemler A Novel Cysteine Cross-linking Method Reveals a Direct Association between Claudin-1 and Tetraspanin CD9 Mol. Cell. Proteomics, November 1, 2007; 6(11): 1855 - 1867. [Abstract] [Full Text] [PDF] V. Barraud-Lange, N. Naud-Barriant, M. Bomsel, J.-P. Wolf, and A. Ziyyat Transfer of oocyte membrane fragments to fertilizing spermatozoa FASEB J, November 1, 2007; 21(13): 3446 - 3449. [Abstract] [Full Text] [PDF] M. Sala-Valdes, A. Ursa, S. Charrin, E. Rubinstein, M. E. Hemler, F. Sanchez-Madrid, and M. Yanez-Mo EWI-2 and EWI-F Link the Tetraspanin Web to the Actin Cytoskeleton through Their Direct Association with Ezrin-Radixin-Moesin Proteins J. Biol. Chem., July 14, 2006; 281(28): 19665 - 19675. [Abstract] [Full Text] [PDF] X. H. Yang, O. V. Kovalenko, T. V. Kolesnikova, M. M. Andzelm, E. Rubinstein, J. L. Strominger, and M. E. Hemler Contrasting Effects of EWI Proteins, Integrins, and Protein Palmitoylation on Cell Surface CD9 Organization J. Biol. Chem., May 5, 2006; 281(18): 12976 - 12985. [Abstract] [Full Text] [PDF] S. Levy and T. Shoham Protein-Protein Interactions in the Tetraspanin Web Physiology, August 1, 2005; 20(4): 218 - 224. [Abstract] [Full Text] [PDF] X. Yang, O. V. Kovalenko, W. Tang, C. Claas, C. S. Stipp, and M. E. Hemler Palmitoylation supports assembly and function of integrin-tetraspanin complexes J. Cell Biol., December 20, 2004; 167(6): 1231 - 1240. [Abstract] [Full Text] [PDF]

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