Specific Residues in a Purine Transporter Are Critical for Dimerization, ER Exit, and Function.

ABSTRACT: Transporters are transmembrane proteins that mediate the selective translocation of solutes across biological membranes. Recently, we have shown that specific interactions with plasma membrane phospholipids are essential for the formation and/or stability of functional dimers of the purine transporter UapA, a prototypic eukaryotic member of the ubiquitous nucleobase ascorbate transporter (NAT) family. Here, we provide strong evidence that distinct interactions of UapA with membrane lipids are essential for ab initio formation of functional dimers in the ER, or ER exit and further subcellular trafficking. Through genetic screens, we identify mutations that restore defects in dimer formation and/or trafficking. Suppressors of defective dimerization restore ab initio formation o

SUBMITTER: Kourkoulou A 

PROVIDER: S-EPMC6893392 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature