A unique PDZ domain and arrestin-like fold interaction reveals mechanistic details of endocytic recycling by SNX27-retromer

Gallon, Matthew, Clairfeuille, Thomas, Steinberg, Florian, Mas, Caroline, Ghai, Rajesh, Sessions, Richard B., Teasdale, Rohan D., Collins, Brett M. and Cullen, Peter J. (2014) A unique PDZ domain and arrestin-like fold interaction reveals mechanistic details of endocytic recycling by SNX27-retromer. Proceedings of the National Academy of Sciences of the United States of America, 111 35: E3604-E3613. doi:10.1073/pnas.1410552111


Author Gallon, Matthew
Clairfeuille, Thomas
Steinberg, Florian
Mas, Caroline
Ghai, Rajesh
Sessions, Richard B.
Teasdale, Rohan D.
Collins, Brett M.
Cullen, Peter J.
Title A unique PDZ domain and arrestin-like fold interaction reveals mechanistic details of endocytic recycling by SNX27-retromer
Journal name Proceedings of the National Academy of Sciences of the United States of America   Check publisher's open access policy
ISSN 0027-8424
1091-6490
Publication date 2014-09-02
Year available 2014
Sub-type Article (original research)
DOI 10.1073/pnas.1410552111
Open Access Status DOI
Volume 111
Issue 35
Start page E3604
End page E3613
Total pages 10
Place of publication Washington, DC, United States
Publisher National Academy of Sciences
Language eng
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 β-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.
Keyword Alzheimer’s disease
Down syndrome
Parkinson disease
Endosomal recycling
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2015 Collection
Institute for Molecular Bioscience - Publications
 
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Created: Wed, 10 Sep 2014, 00:42:01 EST by Susan Allen on behalf of Institute for Molecular Bioscience