Citation

BibTex format

@article{Pyle:2018:10.1016/j.chembiol.2018.03.011,
author = {Pyle, E and Kalli, AC and Amillis, S and Hall, Z and Lau, AM and Hanyaloglu, AC and Diallinas, G and Byrne, B and Politis, A},
doi = {10.1016/j.chembiol.2018.03.011},
journal = {Cell Chemical Biology},
pages = {840--848.e4},
title = {Structural lipids enable the formation of Functional oligomers of the eukaryotic purine symporter UapA},
url = {http://dx.doi.org/10.1016/j.chembiol.2018.03.011},
volume = {25},
year = {2018}
}

RIS format (EndNote, RefMan)

TY  - JOUR
AB - The role of membrane lipids in modulating eukaryotic transporter assembly and function remains unclear. We investigated the effect of membrane lipids in the structure and transport activity of the purine transporter UapA from Aspergillus nidulans. We found that UapA exists mainly as a dimer and that two lipid molecules bind per UapA dimer. We identified three phospholipid classes that co-purified with UapA: phosphatidylcholine, phosphatidylethanolamine (PE), and phosphatidylinositol (PI). UapA delipidation caused dissociation of the dimer into monomers. Subsequent addition of PI or PE rescued the UapA dimer and allowed recovery of bound lipids, suggesting a central role of these lipids in stabilizing the dimer. Molecular dynamics simulations predicted a lipid binding site near the UapA dimer interface. Mutational analyses established that lipid binding at this site is essential for formation of functional UapA dimers. We propose that structural lipids have a central role in the formation of functional, dimeric UapA.
AU - Pyle,E
AU - Kalli,AC
AU - Amillis,S
AU - Hall,Z
AU - Lau,AM
AU - Hanyaloglu,AC
AU - Diallinas,G
AU - Byrne,B
AU - Politis,A
DO - 10.1016/j.chembiol.2018.03.011
EP - 848
PY - 2018///
SN - 2451-9456
SP - 840
TI - Structural lipids enable the formation of Functional oligomers of the eukaryotic purine symporter UapA
T2 - Cell Chemical Biology
UR - http://dx.doi.org/10.1016/j.chembiol.2018.03.011
UR - https://www.ncbi.nlm.nih.gov/pubmed/29681524
UR - http://hdl.handle.net/10044/1/58702
VL - 25
ER -

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