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Originally published In Press as doi:10.1074/jbc.M000829200 on August 23, 2000

J. Biol. Chem., Vol. 275, Issue 47, 36632-36636, November 24, 2000
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Histidine Phosphorylation of Annexin I in Airway Epithelia*

Richmond MuimoDagger §, Zuzanna HornickovaDagger , Claudia E. RiemenDagger , Volker Gerke, Harry Matthews||, and Anil MehtaDagger

From the Dagger  Tayside Institute of Child Health, Ninewells Hospital and Medical School, University of Dundee, Dundee DD1 9SY, United Kingdom, the || Department of Biological Chemistry, University of California, Davis, California 95616, and the  Institue of Medical Biochemistry, University of Münster, von-Esmarch-Strasse 56, D-48149 Münster, Federal Republic Germany

Although [Cl-]i regulates many cellular functions including cell secretion, the mechanisms governing these actions are not known. We have previously shown that the apical membrane of airway epithelium contains a 37-kDa phosphoprotein (p37) whose phosphorylation is regulated by chloride concentration. Using metal affinity (chelating Fe3+-Sepharose) and anion exchange (POROS HQ 20) chromatography, we have purified p37 from ovine tracheal epithelia to electrophoretic homogeneity. Sequence analysis and immunoprecipitation using monoclonal and specific polyclonal antibodies identified p37 as annexin I, a member of a family of Ca2+-dependent phospholipid-binding proteins. Phosphate on [32P]annexin I, phosphorylated using both [gamma -32P]ATP and [gamma -32P]GTP, was labile under acidic but not alkaline conditions. Phosphoamino acid analysis showed the presence of phosphohistidine. The site of phosphorylation was localized to a carboxyl-terminal fragment of annexin I. Our data suggest that cAMP and AMP (but not cGMP) may regulate annexin I histidine phosphorylation. We propose a role for annexin I in an intracellular signaling system involving histidine phosphorylation.

* This work was supported by Wellcome Trust Grant 0044854/Z/95/A, by Biomed II Network Grant BM H4-CT96-0602, and by grants from the Cystic Fibrosis Trust, Tenovus Tayside, the Deutsche Forschungsgemeinschaft, the Royal Society, and the Anonymous Trust.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ To whom correspondence should be addressed. Tel.: 44-1382-660111 (ext. 33055); Fax: 44-1382-632597; E-mail: r.muimo@dundee.ac.uk.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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