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Regulation of the Equilibrium between Closed and Open Conformations of Annexin A2 by N-Terminal Phosphorylation and S100A4-Binding.

Journal article
Authors Péter Ecsédi
Bence Kiss
Gergő Gógl
László Radnai
László Buday
Kitti Koprivanacz
Károly Liliom
Ibolya Leveles
Beáta Vértessy
Norbert Jeszenői
Csaba Hetényi
Gitta Schlosser
Gergely Katona
László Nyitray
Published in Structure (London, England : 1993)
Volume 25
Issue 8
Pages 1195-1207.e5
ISSN 1878-4186
Publication year 2017
Published at Department of Chemistry and Molecular Biology
Pages 1195-1207.e5
Language en
Subject categories Biophysics, Structural Biology, Biochemistry, Biochemistry and Molecular Biology


Annexin A2 (ANXA2) has a versatile role in membrane-associated functions including membrane aggregation, endo- and exocytosis, and it is regulated by post-translational modifications and protein-protein interactions through the unstructured N-terminal domain (NTD). Our sequence analysis revealed a short motif responsible for clamping the NTD to the C-terminal core domain (CTD). Structural studies indicated that the flexibility of the NTD and CTD are interrelated and oppositely regulated by Tyr24 phosphorylation and Ser26Glu phosphomimicking mutation. The crystal structure of the ANXA2-S100A4 complex showed that asymmetric binding of S100A4 induces dislocation of the NTD from the CTD and, similar to the Ser26Glu mutation, unmasks the concave side of ANXA2. In contrast, pTyr24 anchors the NTD to the CTD and hampers the membrane-bridging function. This inhibition can be restored by S100A4 and S100A10 binding. Based on our results we provide a structural model for regulation of ANXA2-mediated membrane aggregation by NTD phosphorylation and S100 binding.

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