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Structural basis for substrate specificity and regulation of nucleotide sugar transporters in the lipid bilayer

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Parker, Joanne L., Corey, Robin A., Stansfeld, Phillip J. and Newstead, Simon (2019) Structural basis for substrate specificity and regulation of nucleotide sugar transporters in the lipid bilayer. Nature Communications, 10 . 4657. doi:10.1038/S41467-019-12673-w

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Official URL: https://doi.org/10.1038/S41467-019-12673-w

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Abstract

Nucleotide sugars are the activated form of monosaccharides used by glycosyltransferases during glycosylation. In eukaryotes the SLC35 family of solute carriers are responsible for their selective uptake into the Endoplasmic Reticulum or Golgi apparatus. The structure of the yeast GDP-mannose transporter, Vrg4, revealed a requirement for short chain lipids and a marked difference in transport rate between the nucleotide sugar and nucleoside monophosphate, suggesting a complex network of regulatory elements control transport into these organelles. Here we report the crystal structure of the GMP bound complex of Vrg4, revealing the molecular basis for GMP recognition and transport. Molecular dynamics, combined with biochemical analysis, reveal a lipid mediated dimer interface and mechanism for coordinating structural rearrangements during transport. Together these results provide further insight into how SLC35 family transporters function within the secretory pathway and sheds light onto the role that membrane lipids play in regulating transport across the membrane.

Item Type: Journal Article
Subjects: Q Science > QH Natural history
Q Science > QP Physiology
Divisions: Faculty of Science, Engineering and Medicine > Science > Chemistry
Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- )
Library of Congress Subject Headings (LCSH): Nucleotides , Glycosylation, Endoplasmic reticulum, Molecular dynamics, Membrane lipids
Journal or Publication Title: Nature Communications
Publisher: Nature Publishing Group
ISSN: 2041-1723
Official Date: 11 October 2019
Dates:
DateEvent
11 October 2019Published
24 September 2019Accepted
Volume: 10
Article Number: 4657
DOI: 10.1038/S41467-019-12673-w
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Open Access
RIOXX Funder/Project Grant:
Project/Grant IDRIOXX Funder NameFunder ID
102890/Z/13/ZWellcome Trusthttp://dx.doi.org/10.13039/100010269
102890/Z/13/AWellcome Trusthttp://dx.doi.org/10.13039/100010269
MR/S021043/1[MRC] Medical Research Councilhttp://dx.doi.org/10.13039/501100000265
208361/Z/17/ZWellcome Trusthttp://dx.doi.org/10.13039/100010269
MR/S009213/1[MRC] Medical Research Councilhttp://dx.doi.org/10.13039/501100000265
BB/P01948X/1[BBSRC] Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
BB/R002517/1[BBSRC] Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
BB/S003339/1[BBSRC] Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
EP/L000253/1[EPSRC] Engineering and Physical Sciences Research Councilhttp://dx.doi.org/10.13039/501100000266
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