TY - JOUR
TI - Transporter oligomerization: Form and function
AU - Alguel, Y.
AU - Cameron, A.D.
AU - Diallinas, G.
AU - Byrne, B.
JO - Biochemical Society Transactions
PY - 2016
VL - 44
TODO - 6
SP - 1737-1744
PB - PORTLAND PRESS LTD
SN - 0300-5127, 1470-8752
TODO - 10.1042/BST20160217
TODO - ABC transporter;  ammonium transporter;  membrane protein;  nucleic acid base;  sweet protein;  transporter protein;  unclassified drug;  carrier protein;  fungal protein;  UAPA protein, Aspergillus nidulans, Article;  Aspergillus nidulans;  complex formation;  conformational transition;  crystal structure;  dimerization;  oligomerization;  priority journal;  protein family;  protein function;  protein structure;  cell membrane;  chemistry;  genetics;  kinetics;  metabolism;  molecular model;  mutation;  protein conformation;  protein multimerization;  transport at the cellular level, Biological Transport;  Cell Membrane;  Fungal Proteins;  Kinetics;  Membrane Transport Proteins;  Models, Molecular;  Mutation;  Protein Conformation;  Protein Multimerization
TODO - 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 the roles of oligomerization in many particularly well-studied transporters and transporter families. © 2016 The Author(s).
ER -