4.5 Article

Analysis of homologous and heterologous interactions between UDP-galactose transporter and beta-1,4-galactosyltransferase 1 using NanoBiT

Journal

ANALYTICAL BIOCHEMISTRY
Volume 593, Issue -, Pages -

Publisher

ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.ab.2020.113599

Keywords

NanoBiT; Split luciferase complementation assay; N-Glycosylation; Golgi apparatus; UDP-Galactose transporter; Beta-1,4-galactosyltransferase 1

Funding

  1. National Science Centre (NCN), Krakow, Poland [2016/23/D/NZ3/01314]

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Split luciferase complementation assay is one of the approaches enabling identification and analysis of protein-protein interactions in vivo. The NanoBiT technology is the most recent improvement of this strategy. Nucleotide sugar transporters and glycosyltransferases of the Golgi apparatus are the key players in glycosylation. Here we demonstrate the applicability of the NanoBiT system for studying homooligomerization of these proteins. We also report and discuss a novel heterologous interaction between UDP-galactose transporter and beta-1,4-galactosyltransferase 1.

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