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Blood, 15 October 2007, Vol. 110, No. 8, pp. 2974-2982. Prepublished online as a Blood First Edition Paper on July 16, 2007; DOI 10.1182/blood-2007-01-065276. This Article Full Text (PDF) All Versions of this Article: blood-2007-01-065276v1 110/8/2974    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 Mody, P. D Articles by Sperling, A. I Search for Related Content PubMed PubMed Citation Articles by Mody, P. D Articles by Sperling, A. I Social Bookmarking                   What's this?  Previous Article  |  Next Article  Submitted January 4, 2007 Accepted June 19, 2007 Signaling through CD43 regulates CD4 T cell trafficking Purvi D Mody, Judy L Cannon, Hozefa S Bandukwala, Kelly M Blaine, Alexander B Schilling, Kevin Swier, and Anne I Sperling* Committee on Immunology, University of Chicago, Chicago, IL, United States Department of Medicine, Section of Pulmonary and Critical Care Medicine, University of Chicago, Chicago, IL, United States Proteomics and Informatics Services Facility, University of Illinois at Chicago, Chicago, IL, United States Department of Biological Sciences, Chicago State University, Chicago, IL, United States * Corresponding author; email: asperlin{at}uchicago.edu. The mucin-like protein CD43 is excluded from the immune synapse, and regulates T cell proliferation as well as T cell migration. While the CD43 cytoplasmic domain is necessary for regulation of T cell activation and proliferation, the mechanism via which CD43 regulates trafficking is not well defined. To investigate whether CD43 phosphorylation regulates its function in T cells, we used tandem mass spectrometry and identified Ser76 in murine CD43 as a previously unidentified site of basal phosphorylation. Interestingly, mutation of this single serine to alanine greatly diminishes T cell trafficking to the lymph node, while CD43 exclusion and CD43-mediated regulation of T cell proliferation remain intact. Further, the CD43 extracellular domain was also required for T cell trafficking, providing a hitherto unknown function for the extracellular domain, and suggesting that the extracellular domain may be required to transduce signals via the cytoplasmic domain. These data reveal a novel mechanism by which CD43 regulates T cell function, and suggest that CD43 functions as a signaling molecule, sensing extracellular cues, and transducing intracellular signals that modulate T cell function. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: M. Matsumoto, M. Miyasaka, and T. Hirata P-Selectin Glycoprotein Ligand-1 Negatively Regulates T-Cell Immune Responses J. Immunol., December 1, 2009; 183(11): 7204 - 7211. [Abstract] [Full Text] [PDF] W. Seo and H. J. Ziltener CD43 processing and nuclear translocation of CD43 cytoplasmic tail are required for cell homeostasis Blood, October 22, 2009; 114(17): 3567 - 3577. [Abstract] [Full Text] [PDF] A. Mambole, D. Baruch, P. Nusbaum, S. Bigot, M. Suzuki, P. Lesavre, M. Fukuda, and L. Halbwachs-Mecarelli The Cleavage of Neutrophil Leukosialin (CD43) by Cathepsin G Releases Its Extracellular Domain and Triggers Its Intramembrane Proteolysis by Presenilin/{gamma}-Secretase J. Biol. Chem., August 29, 2008; 283(35): 23627 - 23635. [Abstract] [Full Text] [PDF]

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