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

  • Ali Reza Nazmi , Gabriel Ozorowski , Milena Pejic , Julian P. Whitelegge , Volker Gerke EMAIL logo and Hartmut Luecke EMAIL logo
Published/Copyright: September 8, 2012
Biological Chemistry
From the journal Biological Chemistry Volume 393 Issue 10

Abstract

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
Corresponding authors: Volker Gerke and Hartmut Luecke, Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697-3900, USA
Received: 2012-4-16
Accepted: 2012-7-12
Published Online: 2012-09-08
Published in Print: 2012-10-01

©2012 by Walter de Gruyter Berlin Boston

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https://doi.org/10.1515/hsz-2012-0179
Keywords for this article
annexin; calcium; membrane binding; prokaryotic post-translational modification; protein interaction; Robert Huber

Articles in the same Issue

  1. Masthead
  2. Masthead
  3. Guest Editorial
  4. No end in sight: the development of protein crystallography in Martinsried
  5. Highlight: No End in Sight: The Development of Protein Crystallography in Martinsried
  6. Functional and structural insights into astacin metallopeptidases
  7. β-Trefoil inhibitors – from the work of Kunitz onward
  8. Structural basis of the TAL effector–DNA interaction
  9. Nature’s way of handling a greenhouse gas: the copper-sulfur cluster of purple nitrous oxide reductase
  10. Rustless translation
  11. Structural basis of [NiFe] hydrogenase maturation by Hyp proteins
  12. Covalent and non-covalent reversible proteasome inhibition
  13. Structural origins of AGC protein kinase inhibitor selectivities: PKA as a drug discovery tool
  14. Structural analysis of the C-terminal domain of the spliceosomal helicase Prp22
  15. N-terminal acetylation of annexin A2 is required for S100A10 binding
  16. Withaferin A binds covalently to the N-terminal domain of annexin A2
  17. PhoB transcriptional activator binds hierarchically to pho box promoters
  18. Research Articles/Short Communications
  19. Protein Structure and Function
  20. Biochemical and functional characterization of human phospholipid scramblase 4 (hPLSCR4)
  21. Cell Biology and Signaling
  22. Dual-specificity phosphatases are targets of the Wnt/β-catenin pathway and candidate mediators of β-catenin/Ras signaling interactions
  23. Proteolysis
  24. Inhibition of Aeromonas sobria serine protease (ASP) by α2-macroglobulin
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