Title |
A molecular code for endosomal recycling of phosphorylated cargos by the SNX27–retromer complex
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Published in |
Nature Structural & Molecular Biology, September 2016
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DOI | 10.1038/nsmb.3290 |
Pubmed ID | |
Authors |
Thomas Clairfeuille, Caroline Mas, Audrey S M Chan, Zhe Yang, Maria Tello-Lafoz, Mintu Chandra, Jocelyn Widagdo, Markus C Kerr, Blessy Paul, Isabel Mérida, Rohan D Teasdale, Nathan J Pavlos, Victor Anggono, Brett M Collins |
Abstract |
Recycling of internalized receptors from endosomal compartments is essential for the receptors' cell-surface homeostasis. Sorting nexin 27 (SNX27) cooperates with the retromer complex in the recycling of proteins containing type I PSD95-Dlg-ZO1 (PDZ)-binding motifs. Here we define specific acidic amino acid sequences upstream of the PDZ-binding motif required for high-affinity engagement of the human SNX27 PDZ domain. However, a subset of SNX27 ligands, such as the β2 adrenergic receptor and N-methyl-D-aspartate (NMDA) receptor, lack these sequence determinants. Instead, we identified conserved sites of phosphorylation that substitute for acidic residues and dramatically enhance SNX27 interactions. This newly identified mechanism suggests a likely regulatory switch for PDZ interaction and protein transport by the SNX27-retromer complex. Defining this SNX27 binding code allowed us to classify more than 400 potential SNX27 ligands with broad functional implications in signal transduction, neuronal plasticity and metabolite transport. |
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Australia | 1 | 100% |
Demographic breakdown
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Members of the public | 1 | 100% |
Mendeley readers
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Student > Ph. D. Student | 33 | 22% |
Student > Master | 18 | 12% |
Student > Bachelor | 16 | 11% |
Researcher | 15 | 10% |
Student > Doctoral Student | 7 | 5% |
Other | 22 | 15% |
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Immunology and Microbiology | 3 | 2% |
Other | 9 | 6% |
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