In situ dimerization of multiple wild type and mutant zinc transporters in live cells using bimolecular fluorescence complementation.

ABSTRACT: Zinc transporters (ZnTs) facilitate zinc efflux and zinc compartmentalization, thereby playing a key role in multiple physiological processes and pathological disorders, presumed to be modulated by transporter dimerization. We recently proposed that ZnT2 homodimerization is the underlying basis for the dominant negative effect of a novel heterozygous G87R mutation identified in women producing zinc-deficient milk. To provide direct visual evidence for the in situ dimerization and function of multiple normal and mutant ZnTs, we applied here the bimolecular fluorescence complementation (BiFC) technique, which enables direct visualization of specific protein-protein interactions. BiFC is based upon reconstitution of an intact fluorescent protein including YFP when its two complementary, non-f

SUBMITTER: Lasry I 

PROVIDER: S-EPMC3953246 | biostudies-literature | 2014 Mar

REPOSITORIES: biostudies-literature