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Blood, 1 May 2005, Vol. 105, No. 9, pp. 3663-3670. Prepublished online as a Blood First Edition Paper on January 18, 2005; DOI 10.1182/blood-2004-08-3325. This Article Full Text (PDF) All Versions of this Article: 2004-08-3325v1 105/9/3663    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 Bannas, P. Articles by Koch-Nolte, F. Search for Related Content PubMed PubMed Citation Articles by Bannas, P. Articles by Koch-Nolte, F. Social Bookmarking                   What's this?  Previous Article  |  Next Article  Submitted August 26, 2004 Accepted January 7, 2005 Activity and specifity of toxin-related mouse T cell ecto-ADP-ribosyltransferase ART2.2 depends on its association with lipid rafts Peter Bannas, Sahil Adriouch, Sarah Kahl, Fenja Braasch, Friedrich Haag, and Friedrich Koch-Nolte* Institute of Immunology, University Hospital, Hamburg, Germany * Corresponding author; email: nolte{at}uke.uni-hamburg.de. ADP-ribosyltransferases (ARTs) transfer ADP-ribose from NAD onto target proteins. T cells express ART2.2, a toxin-related, GPI-anchored ecto-enzyme. Following release of NAD from cells, ART2.2 ADP-ribosylates the P2X7 purinoceptor, lymphocyte function associated antigen (LFA-1), and other membrane proteins. Using lymphoma transfectants expressing either ART2.2 with its native GPI-anchor (ART2.2-GPI) or ART2.2 with a grafted transmembane anchor (ART2.2-Tm) we demonstrate that ART2.2-GPI but not ART2.2-Tm associates with glycosphingolipid enriched microdomains (lipid rafts). At limiting substrate concentrations ART2.2-GPI exhibits a more than 10-fold higher activity than ART2.2-Tm. On intact cells ART2.2-GPI ADP-ribosylates a small number of distinct target proteins. Strikingly, disruption of lipid rafts by cyclodextrin or membrane solubilization by Triton X-100 increases the spectrum of modified target proteins. However, ART2.2 itself is a prominent target for ADP-ribosylation only when GPI-anchored. Furthermore, cholesterol depletion or detergent solubilization abolishes auto-ADP-ribosylation of ART2.2. These findings imply that ART2.2-GPI but not ART2.2-Tm molecules are closely associated on the plasma membrane and lend support to the hypothesis that lipid rafts exist on living cells as platforms to which certain proteins are admitted and others are excluded. Our results further suggest that raft association focuses ART2.2 on specific targets that constitutively or inducible associate with lipid rafts. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: S. Adriouch, P. Bannas, N. Schwarz, R. Fliegert, A. H. Guse, M. Seman, F. Haag, and F. Koch-Nolte ADP-ribosylation at R125 gates the P2X7 ion channel by presenting a covalent ligand to its nucleotide binding site FASEB J, March 1, 2008; 22(3): 861 - 869. [Abstract] [Full Text] [PDF] F. Koch-Nolte, J. Reyelt, B. Schossow, N. Schwarz, F. Scheuplein, S. Rothenburg, F. Haag, V. Alzogaray, A. Cauerhff, and F. A. Goldbaum Single domain antibodies from llama effectively and specifically block T cell ecto-ADP-ribosyltransferase ART2.2 in vivo FASEB J, November 1, 2007; 21(13): 3490 - 3498. [Abstract] [Full Text] [PDF] S. Adriouch, S. Hubert, S. Pechberty, F. Koch-Nolte, F. Haag, and M. Seman NAD+ Released during Inflammation Participates in T Cell Homeostasis by Inducing ART2-Mediated Death of Naive T Cells In Vivo J. Immunol., July 1, 2007; 179(1): 186 - 194. [Abstract] [Full Text] [PDF] C. M. Cruz, A. Rinna, H. J. Forman, A. L. M. Ventura, P. M. Persechini, and D. M. Ojcius ATP Activates a Reactive Oxygen Species-dependent Oxidative Stress Response and Secretion of Proinflammatory Cytokines in Macrophages J. Biol. Chem., February 2, 2007; 282(5): 2871 - 2879. [Abstract] [Full Text] [PDF] S. D. Liao and D. G. Puro NAD+-Induced Vasotoxicity in the Pericyte-Containing Microvasculature of the Rat Retina: Effect of Diabetes Invest. Ophthalmol. Vis. Sci., November 1, 2006; 47(11): 5032 - 5038. [Abstract] [Full Text] [PDF] M. Garcia-Marcos, E. Perez-Andres, S. Tandel, U. Fontanils, A. Kumps, E. Kabre, A. Gomez-Munoz, A. Marino, J.-P. Dehaye, and S. Pochet Coupling of two pools of P2X7 receptors to distinct intracellular signaling pathways in rat submandibular gland J. Lipid Res., April 1, 2006; 47(4): 705 - 714. [Abstract] [Full Text] [PDF]

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