Structure of the endocytic adaptor complex reveals the basis for efficient membrane anchoring during clathrin-mediated endocytosis
| العنوان: | Structure of the endocytic adaptor complex reveals the basis for efficient membrane anchoring during clathrin-mediated endocytosis |
|---|---|
| المؤلفون: | Michal Skruzny, Dmitri I. Svergun, David P. Klebl, Roland Thuenauer, Katharina Veith, Maria Garcia-Alai, Stephen P. Muench, Stephan Niebling, Haydyn D. T. Mertens, Frank Sobott, Marc Abella, Javier Lizarrondo, Martin A. Schroer |
| المصدر: | Nature communications Nature Communications Nature Communications 12(1), 2889 (1-15) (2021). doi:10.1038/s41467-021-23151-7 Nature Communications, Vol 12, Iss 1, Pp 1-15 (2021) |
| سنة النشر: | 2021 |
| مصطلحات موضوعية: | 0301 basic medicine, Models, Molecular, Saccharomyces cerevisiae Proteins, Science, Endocytic cycle, Vesicular Transport Proteins, General Physics and Astronomy, Saccharomyces cerevisiae, macromolecular substances, Endocytosis, General Biochemistry, Genetics and Molecular Biology, Article, 03 medical and health sciences, 0302 clinical medicine, Tetramer, Biology, Membrane invagination, Multidisciplinary, Binding Sites, Chemistry, Mutagenesis, Cell Membrane, Cryoelectron Microscopy, General Chemistry, Receptor-mediated endocytosis, SAXS, Actin cytoskeleton, In vitro, Clathrin, Protein Structure, Tertiary, Adaptor Proteins, Vesicular Transport, Cytoskeletal Proteins, 030104 developmental biology, Membrane, Biophysics, ddc:500, Protein Multimerization, Engineering sciences. Technology, 030217 neurology & neurosurgery |
| الوصف: | Nature Communications 12(1), 2889 (1-15) (2021). doi:10.1038/s41467-021-23151-7 During clathrin-mediated endocytosis, a complex and dynamic network of protein-membrane interactions cooperate to achieve membrane invagination. Throughout this process in yeast, endocytic coat adaptors, Sla2 and Ent1, must remain attached to the plasma membrane to transmit force from the actin cytoskeleton required for successful membrane invagination. Here, we present a cryo-EM structure of a 16-mer complex of the ANTH and ENTH membrane-binding domains from Sla2 and Ent1 bound to PIP$_2$ that constitutes the anchor to the plasma membrane. Detailed in vitro and in vivo mutagenesis of the complex interfaces delineate the key interactions for complex formation and deficient cell growth phenotypes demonstrate its biological relevance. A hetero-tetrameric unit binds PIP$_2$ molecules at the ANTH-ENTH interfaces and can form larger assemblies to contribute to membrane remodeling. Finally, a time-resolved small-angle X-ray scattering study of the interaction of these adaptor domains in vitro suggests that ANTH and ENTH domains have evolved to achieve a fast subsecond timescale assembly in the presence of PIP$_2$ and do not require further proteins to form a stable complex. Together, these findings provide a molecular understanding of an essential piece in the molecular puzzle of clathrin-coated endocytic sites. Published by Nature Publishing Group UK, [London] |
| وصف الملف: | application/pdf |
| اللغة: | English |
| تدمد: | 2041-1723 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a5bdbcb7405c8495cdfe1fbab1c0048 https://hdl.handle.net/10067/1796100151162165141 |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....3a5bdbcb7405c8495cdfe1fbab1c0048 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 20411723 |
|---|