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Blood, 15 May 2005, Vol. 105, No. 10, pp. 4088-4095. Prepublished online as a Blood First Edition Paper on February 3, 2005; DOI 10.1182/blood-2004-05-1895. This Article Full Text Full Text (PDF) Supplemental Figure All Versions of this Article: 2004-05-1895v1 105/10/4088    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map 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 Toye, A. M. Articles by Tanner, M. J. A. Search for Related Content PubMed PubMed Citation Articles by Toye, A. M. Articles by Tanner, M. J. A. Related Collections Red Cells Cytoskeleton Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  RED CELLS Protein-4.2 association with band 3 (AE1, SLCA4) in Xenopus oocytes: effects of three natural protein-4.2 mutations associated with hemolytic anemia Ashley M. Toye, Sandip Ghosh, Mark T. Young, Graham K. Jones, Richard B. Sessions, Martine Ramaugé, Philippe Leclerc, Joyoti Basu, Jean Delaunay, and Michael J. A. Tanner From the Department of Biochemistry, University of Bristol, School of Medical Sciences, Bristol, United Kingdom; L'Institut National de la Santé et de la Recherche Médicale (INSERM) U 473, Service d'Hématologie, Hôpital de Bicêtre, Assistance Publique-Hôpitaux de Paris, and Faculté de Médecine Paris-Sud, Le Kremlin-Bicêtre, France; Department of Chemistry, Bose Institute, Calcutta, India; and INSERM U 488, Le Kremlin-Bicêtre, France. We have investigated the effects of coexpression of protein 4.2 and three protein-4.2 variants with band 3 in the Xenopus oocyte expression system. Normal protein 4.2 increased band-3–specific chloride transport in the oocytes. Protein 4.2 also coimmunoprecipitated with band 3 and colocalized with band 3 at the oocyte plasma membrane. The increase in band-3–mediated chloride transport and coimmunoprecipitation of protein 4.2 required the presence of the N-terminal cytoplasmic domain of band 3. Protein 4.2 also localized to the oocyte plasma membrane in the absence of band 3. The protein-4.2 variants 4.2 Tozeur (R310Q) and 4.2 Komatsu (D175Y) had impaired ability to bind to band 3 and these variants did not localize to the oocyte plasma membrane when expressed on their own or when coexpressed with band 3. Unexpectedly, 4.2 Nippon (A142T) behaved similarly to normal protein 4.2. In the absence of a crystal structure of protein 4.2, we propose a homology model of protein 4.2 based on the structure of the sequence-related protein transglutaminase. Using our results in oocytes and this homology model we speculate how these mutations affect protein 4.2 and result in hereditary spherocytosis. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: S. E. Iismaa, B. M. Mearns, L. Lorand, and R. M. Graham Transglutaminases and Disease: Lessons From Genetically Engineered Mouse Models and Inherited Disorders Physiol Rev, July 1, 2009; 89(3): 991 - 1023. [Abstract] [Full Text] [PDF] S. L. Alper Molecular physiology and genetics of Na+-independent SLC4 anion exchangers J. Exp. Biol., June 1, 2009; 212(11): 1672 - 1683. [Abstract] [Full Text] [PDF]

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