Cargando…
The S100A10-Annexin A2 Complex Provides a Novel Asymmetric Platform for Membrane Repair
Membrane repair is mediated by multiprotein complexes, such as that formed between the dimeric EF-hand protein S100A10, the calcium- and phospholipid-binding protein annexin A2, the enlargeosome protein AHNAK, and members of the transmembrane ferlin family. Although interactions between these protei...
Autores principales: | , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Society for Biochemistry and Molecular Biology
2011
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3220529/ https://www.ncbi.nlm.nih.gov/pubmed/21949189 http://dx.doi.org/10.1074/jbc.M111.244038 |
_version_ | 1782216973540655104 |
---|---|
author | Rezvanpour, Atoosa Santamaria-Kisiel, Liliana Shaw, Gary S. |
author_facet | Rezvanpour, Atoosa Santamaria-Kisiel, Liliana Shaw, Gary S. |
author_sort | Rezvanpour, Atoosa |
collection | PubMed |
description | Membrane repair is mediated by multiprotein complexes, such as that formed between the dimeric EF-hand protein S100A10, the calcium- and phospholipid-binding protein annexin A2, the enlargeosome protein AHNAK, and members of the transmembrane ferlin family. Although interactions between these proteins have been shown, little is known about their structural arrangement and mechanisms of formation. In this work, we used a non-covalent complex between S100A10 and the N terminus of annexin A2 (residues 1–15) and a designed hybrid protein (A10A2), where S100A10 is linked in tandem to the N-terminal region of annexin A2, to explore the binding region, stoichiometry, and affinity with a synthetic peptide from the C terminus of AHNAK. Using multiple biophysical methods, we identified a novel asymmetric arrangement between a single AHNAK peptide and the A10A2 dimer. The AHNAK peptide was shown to require the annexin A2 N terminus, indicating that the AHNAK binding site comprises regions on both S100A10 and annexin proteins. NMR spectroscopy was used to show that the AHNAK binding surface comprised residues from helix IV in S100A10 and the C-terminal portion from the annexin A2 peptide. This novel surface maps to the exposed side of helices IV and IV′ of the S100 dimeric structure, a region not identified in any previous S100 target protein structures. The results provide the first structural details of the ternary S100A10 protein complex required for membrane repair. |
format | Online Article Text |
id | pubmed-3220529 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | American Society for Biochemistry and Molecular Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-32205292011-11-23 The S100A10-Annexin A2 Complex Provides a Novel Asymmetric Platform for Membrane Repair Rezvanpour, Atoosa Santamaria-Kisiel, Liliana Shaw, Gary S. J Biol Chem Protein Structure and Folding Membrane repair is mediated by multiprotein complexes, such as that formed between the dimeric EF-hand protein S100A10, the calcium- and phospholipid-binding protein annexin A2, the enlargeosome protein AHNAK, and members of the transmembrane ferlin family. Although interactions between these proteins have been shown, little is known about their structural arrangement and mechanisms of formation. In this work, we used a non-covalent complex between S100A10 and the N terminus of annexin A2 (residues 1–15) and a designed hybrid protein (A10A2), where S100A10 is linked in tandem to the N-terminal region of annexin A2, to explore the binding region, stoichiometry, and affinity with a synthetic peptide from the C terminus of AHNAK. Using multiple biophysical methods, we identified a novel asymmetric arrangement between a single AHNAK peptide and the A10A2 dimer. The AHNAK peptide was shown to require the annexin A2 N terminus, indicating that the AHNAK binding site comprises regions on both S100A10 and annexin proteins. NMR spectroscopy was used to show that the AHNAK binding surface comprised residues from helix IV in S100A10 and the C-terminal portion from the annexin A2 peptide. This novel surface maps to the exposed side of helices IV and IV′ of the S100 dimeric structure, a region not identified in any previous S100 target protein structures. The results provide the first structural details of the ternary S100A10 protein complex required for membrane repair. American Society for Biochemistry and Molecular Biology 2011-11-18 2011-09-26 /pmc/articles/PMC3220529/ /pubmed/21949189 http://dx.doi.org/10.1074/jbc.M111.244038 Text en © 2011 by The American Society for Biochemistry and Molecular Biology, Inc. Author's Choice—Final version full access. Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/) applies to Author Choice Articles |
spellingShingle | Protein Structure and Folding Rezvanpour, Atoosa Santamaria-Kisiel, Liliana Shaw, Gary S. The S100A10-Annexin A2 Complex Provides a Novel Asymmetric Platform for Membrane Repair |
title | The S100A10-Annexin A2 Complex Provides a Novel Asymmetric Platform for Membrane Repair |
title_full | The S100A10-Annexin A2 Complex Provides a Novel Asymmetric Platform for Membrane Repair |
title_fullStr | The S100A10-Annexin A2 Complex Provides a Novel Asymmetric Platform for Membrane Repair |
title_full_unstemmed | The S100A10-Annexin A2 Complex Provides a Novel Asymmetric Platform for Membrane Repair |
title_short | The S100A10-Annexin A2 Complex Provides a Novel Asymmetric Platform for Membrane Repair |
title_sort | s100a10-annexin a2 complex provides a novel asymmetric platform for membrane repair |
topic | Protein Structure and Folding |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3220529/ https://www.ncbi.nlm.nih.gov/pubmed/21949189 http://dx.doi.org/10.1074/jbc.M111.244038 |
work_keys_str_mv | AT rezvanpouratoosa thes100a10annexina2complexprovidesanovelasymmetricplatformformembranerepair AT santamariakisielliliana thes100a10annexina2complexprovidesanovelasymmetricplatformformembranerepair AT shawgarys thes100a10annexina2complexprovidesanovelasymmetricplatformformembranerepair AT rezvanpouratoosa s100a10annexina2complexprovidesanovelasymmetricplatformformembranerepair AT santamariakisielliliana s100a10annexina2complexprovidesanovelasymmetricplatformformembranerepair AT shawgarys s100a10annexina2complexprovidesanovelasymmetricplatformformembranerepair |