Distinct Ubiquitin Binding Modes Exhibited by SH3 Domains: Molecular Determinants and Functional Implications
| العنوان: | Distinct Ubiquitin Binding Modes Exhibited by SH3 Domains: Molecular Determinants and Functional Implications |
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| المؤلفون: | Jerónimo Bravo, Martin Blackledge, Ana I. Azuaga, Salvador Casares, Jose L. Ortega Roldan, Nico A. J. van Nuland, Malene Ringkjøbing Jensen, Nayra Cardenes |
| المساهمون: | Institut de biologie structurale (IBS - UMR 5075 ), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Structural Biology Brussels, Department of Bio-engineering Sciences, Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA) |
| المصدر: | Digital.CSIC. Repositorio Institucional del CSIC instname PLoS ONE PLoS ONE, Public Library of Science, 2013, 8 (9), pp.e73018. ⟨10.1371/journal.pone.0073018⟩ PLoS ONE, Vol 8, Iss 9, p e73018 (2013) Digibug. Repositorio Institucional de la Universidad de Granada PLoS ONE, 2013, 8 (9), pp.e73018. ⟨10.1371/journal.pone.0073018⟩ |
| بيانات النشر: | Public Library of Science, 2013. |
| سنة النشر: | 2013 |
| مصطلحات موضوعية: | Models, Molecular, Ubiquitin binding, MESH: Cytoskeletal Proteins, Protein Conformation, 01 natural sciences, environment and public health, SH3 domain, Nuclear magnetic resonance, Crystal structure refinement, Protein structure, MESH: Protein Conformation, Ubiquitin, MESH: Nuclear Magnetic Resonance, Biomolecular, Genetics, 0303 health sciences, Multidisciplinary, biology, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], 3. Good health, Ubiquitin ligase, Cell biology, CIN85/CD2AP/CMS, Medicine, MESH: Models, Molecular, Binding domain, Protein Binding, Research Article, animal structures, MESH: Mutation, MESH: Ubiquitin, Phenylalanine, Science, Protein domain, macromolecular substances, 010402 general chemistry, MESH: src Homology Domains, Protein–protein interaction, src Homology Domains, 03 medical and health sciences, ubiquitin, Binding analysis, MESH: Protein Binding, Protein Interaction Domains and Motifs, Nuclear Magnetic Resonance, Biomolecular, 030304 developmental biology, Adaptor Proteins, Signal Transducing, MESH: Adaptor Proteins, Signal Transducing, MESH: Protein Interaction Domains and Motifs, Crystal structure, Ubiquitination, Protein interactions, NMR, 0104 chemical sciences, Cytoskeletal Proteins, Mutation, SH3 domains, biology.protein, Tyrosine |
| الوصف: | 14 páginas, 6 figuras. En material suplementario: 3 figuras, 2 tablas SH3 domains constitute a new type of ubiquitin-binding domains. We previously showed that the third SH3 domain (SH3-C) of CD2AP binds ubiquitin in an alternative orientation. We have determined the structure of the complex between first CD2AP SH3 domain and ubiquitin and performed a structural and mutational analysis to decipher the determinants of the SH3-C binding mode to ubiquitin. We found that the Phe-to-Tyr mutation in CD2AP and in the homologous CIN85 SH3-C domain does not abrogate ubiquitin binding, in contrast to previous hypothesis and our findings for the first two CD2AP SH3 domains. The similar alternative binding mode of the SH3-C domains of these related adaptor proteins is characterised by a higher affinity to C-terminal extended ubiquitin molecules. We conclude that CD2AP/CIN85 SH3-C domain interaction with ubiquitin constitutes a new ubiquitin-binding mode involved in a different cellular function and thus changes the previously established mechanism of EGF-dependent CD2AP/CIN85 mono-ubiquitination. This research was funded by grant BIO2005-04650 from the Spanish Ministry of Education and Science (MEC) and FQM-02838 from the Andalucia Regional Government. Work at J.B. laboratory was funded by the Spanish Ministry of Education and Innovation (SAF2009-10667). J.L.O.R. is supported by a Federation of European Biochemical Societies (FEBS) post-doctoral grant. S.C.A. is supported by a resettlement contract from the University of Granada. N.A.J.v.N is a group leader of the Vlaams Instituut voor Biotechnologie (VIB). The 600 MHz spectra were recorded in the Centre for Scientific Instrumentation (CIC) of the University of Granada and at the RALF Large Scale Facility in Grenoble, which is funded by the 'Access to Research Infrastructures' program of the European Union. |
| وصف الملف: | application/pdf |
| تدمد: | 1932-6203 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ae08e2075a94efa9026ee2a370fc57a2Test http://hdl.handle.net/10261/82349Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....ae08e2075a94efa9026ee2a370fc57a2 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 19326203 |
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