期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 23, 期 10, 页码 921-932出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.3290
关键词
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资金
- Australian Research Council (ARC) [DP0985029]
- National Health and Medical Research Council (NHMRC) [APP1042082, APP1058734, APP1078280]
- UWA-UQ Bilateral Research Collaboration Award
- John T. Reid Charitable Trusts
- University of Queensland Postdoctoral Fellowship
- NHMRC [APP1041929, APP1061574]
- ARC [FT100100027]
- FPI fellowship from the Spanish Ministry of Economy and Competitiveness
- Spanish Ministry of Economy and Competitiveness [BFU2013-47640-P]
- Madrid regional government (IMMUNOTHERCAM Consortium) [S2010/BMD-2326]
- Australian Research Council [DP0985029] Funding Source: Australian Research Council
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-DIg-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 beta(2) 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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