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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred

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N-terminal acetylation of annexin A2 is required for S100A10 binding

Ali Reza Nazmi1, a / Gabriel Ozorowski2, a / Milena Pejic1 / Julian P. Whitelegge3 / 1, 2 / 2, 4, 5, 6

1Institute of Medical Biochemistry, ZMBE, University of Münster, von-Esmarch-Str. 56, D-48149 Münster, Germany

2Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697-3900, USA

3The Pasarow Mass Spectrometry Laboratory, The NPI-Semel Institute, David Geffen School of Medicine, University of California, Los Angeles, CA 90024, USA

4Department of Physiology and Biophysics, University of California, Irvine, CA 92697, USA

5Department of Computer Science, University of California, Irvine, CA 92697, USA

6Center for Biomembrane Systems, University of California, Irvine, CA

aThese authors contributed equally to this work.

Corresponding authors: Volker Gerke and Hartmut Luecke, Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697-3900, USA

Citation Information: . Volume 393, Issue 10, Pages 1141–1150, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: 10.1515/hsz-2012-0179, September 2012

Publication History

Published Online:


Annexin A2 (AnxA2), a Ca2+-regulated phospholipid binding protein involved in membrane-cytoskeleton contacts and membrane transport, exists in two physical states, as a monomer or in a heterotetrameric complex mediated by S100A10. Formation of the AnxA2-S100A10 complex is of crucial regulatory importance because only the complex is firmly anchored in the plasma membrane, where it functions in the plasma membrane targeting/recruitment of certain ion channels and receptors. The S100A10 binding motif is located in the first 12 residues of the AnxA2 N-terminal domain, but conflicting reports exist as to the importance of N-terminal AnxA2 acetylation with regard to S100A10 binding. We show here that AnxA2 is subject to N-terminal modification when expressed heterologously in Escherichia coli. Met1 is removed and Ser2 is acetylated, yielding the same modification as the authentic mammalian protein. Bacterially expressed and N-terminally acetylated AnxA2 binds S100A10 with an affinity comparable to AnxA2 from porcine tissue and is capable of forming the AnxA2-S100A10 heterotetramer. Complex formation is competitively inhibited by acetylated but not by non-acetylated peptides covering the N-terminal AnxA2 sequence. These results demonstrate that N-terminal acetylation of AnxA2 is required for S100A10 binding and that this common eukaryotic modification is also obtained upon expression in bacteria.

Keywords: annexin; calcium; membrane binding; prokaryotic post-translational modification; protein interaction; Robert Huber

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