Imperial College London

ProfessorBernadetteByrne

Faculty of Natural SciencesDepartment of Life Sciences

Professor of Molecular Membrane Biology
 
 
 
//

Contact

 

+44 (0)20 7594 3004b.byrne Website

 
 
//

Location

 

504Sir Ernst Chain BuildingSouth Kensington Campus

//

Summary

 

Publications

Citation

BibTex format

@article{Alguel:2016:10.1042/BST20160217,
author = {Alguel, Y and Cameron, AD and Diallinas, G and Byrne, B},
doi = {10.1042/BST20160217},
journal = {Biochemical Society Transactions},
pages = {1737--1744},
title = {Transporter oligomerisation: form and function},
url = {http://dx.doi.org/10.1042/BST20160217},
volume = {44},
year = {2016}
}

RIS format (EndNote, RefMan)

TY  - JOUR
AB - Transporters are integral membrane proteins with central roles in the efficient movement of molecules across biological membranes. Many transporters exist as oligomers in the membrane. Depending on the individual transport protein, oligomerization can have roles in membrane trafficking, function, regulation and turnover. For example, our recent studies on UapA, a nucleobase ascorbate transporter, from Aspergillus nidulans, have revealed both that dimerization of this protein is essential for correct trafficking to the membrane and the structural basis of how one UapA protomer can affect the function of the closely associated adjacent protomer. Here we review roles of oligomerisation in a number of particularly well-studied transporters and transporter families.
AU - Alguel,Y
AU - Cameron,AD
AU - Diallinas,G
AU - Byrne,B
DO - 10.1042/BST20160217
EP - 1744
PY - 2016///
SN - 1470-8752
SP - 1737
TI - Transporter oligomerisation: form and function
T2 - Biochemical Society Transactions
UR - http://dx.doi.org/10.1042/BST20160217
UR - http://hdl.handle.net/10044/1/40359
VL - 44
ER -