PubAg

Main content area

Short N-terminal region of UDP-galactose transporter (SLC35A2) is crucial for galactosylation of N-glycans

Author:
Sosicka, Paulina, Jakimowicz, Piotr, Olczak, Teresa, Olczak, Mariusz
Source:
Biochemical and biophysical research communications 2014 v.454 pp. 486-492
ISSN:
0006-291X
Subject:
Golgi apparatus, humans, recombinant fusion proteins
Abstract:
UDP-galactose transporter (UGT) and UDP-N-acetylglucosamine transporter (NGT) form heterologous complexes in the Golgi apparatus (GA) membrane. We aimed to identify UGT region responsible for galactosylation of N-glycans. Chimeric proteins composed of human UGT and either NGT or CMP-sialic acid transporter (CST) localized to the GA, and all but UGT/CST chimera corrected galactosylation defect in UGT-deficient cell lines, although at different efficiency. Importantly, short N-terminal region composed of 35 N-terminal amino-acid residues of UGT was crucial for galactosylation of N-glycans. The remaining molecule must be derived from NGT not CST, confirming that the role played by UGT and NGT is coupled.
Agid:
5330940