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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Teasdale, Rohan D. Steinberg, Florian Sessions, Richard B. Gallon, Matthew Collins, Brett M. Mas, Caroline Ghai, Rajesh Cullen, Peter J. Clairfeuille, Thomas |
| Description | Author Affiliation: Gallon M ( The Henry Wellcome Integrated Signalling Laboratories, School of Biochemistry, University of Bristol, Bristol BS8 1TD, United Kingdom); Clairfeuille T ( Institute for Molecular Bioscience, University of Queensland, St. Lucia, QLD 4072, Australia); Steinberg F ( The Henry Wellcome Integrated Signalling Laboratories, School of Biochemistry, University of Bristol, Bristol BS8 1TD, United Kingdom); Mas C ( Institute for Molecular Bioscience, University of Queensland, St. Lucia, QLD 4072, Australia); Ghai R ( Institute for Molecular Bioscience, University of Queensland, St. Lucia, QLD 4072, Australia); Sessions RB ( School of Biochemistry, University of Bristol, Bristol BS8 1TD, United Kingdom.); Teasdale RD ( Institute for Molecular Bioscience, University of Queensland, St. Lucia, QLD 4072, Australia); Collins BM ( Institute for Molecular Bioscience, University of Queensland, St. Lucia, QLD 4072, Australia); Cullen PJ ( The Henry Wellcome Integrated Signalling Laboratories, School of Biochemistry, University of Bristol, Bristol BS8 1TD, United Kingdom); |
| Abstract | The sorting nexin 27 (SNX27)-retromer complex is a major regulator of endosome-to-plasma membrane recycling of transmembrane cargos that contain a PSD95, Dlg1, zo-1 (PDZ)-binding motif. Here we describe the core interaction in SNX27-retromer assembly and its functional relevance for cargo sorting. Crystal structures and NMR experiments reveal that an exposed ß-hairpin in the SNX27 PDZ domain engages a groove in the arrestin-like structure of the vacuolar protein sorting 26A (VPS26A) retromer subunit. The structure establishes how the SNX27 PDZ domain simultaneously binds PDZ-binding motifs and retromer-associated VPS26. Importantly, VPS26A binding increases the affinity of the SNX27 PDZ domain for PDZ- binding motifs by an order of magnitude, revealing cooperativity in cargo selection. With disruption of SNX27 and retromer function linked to synaptic dysfunction and neurodegenerative disease, our work provides the first step, to our knowledge, in the molecular description of this important sorting complex, and more broadly describes a unique interaction between a PDZ domain and an arrestin-like fold. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 35 |
| Volume Number | 111 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2014-09-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Endocytosis Physiology PDZ Domains Genetics Sorting Nexins Chemistry Vesicular Transport Proteins Amino Acid Sequence Animals Arrestin Brain Diseases Metabolism Pathology Crystallography, X-Ray Endosomes HEK293 Cells Mice Molecular Sequence Data Mutagenesis Nerve Tissue Proteins Protein Folding Protein Sorting Signals RNA, Small Interfering Sequence Homology, Amino Acid Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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