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Updated: May 28, 2025

Demonstration of Heterologous Complexes formed by Golgi-Resident Type III Membrane Proteins using Split Luciferase Complementation Assay
Published on: September 10, 2020
Multiprotein Complexes of Plant Glycosyltransferases Involved in Their Function and Trafficking
Ning Zhang1, Jordan D Julian1, Olga A Zabotina1
1Roy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA 50011, USA.
Abstract:
Plant cells utilize protein oligomerization for their functions in numerous important cellular processes. Protein-protein interactions are necessary to stabilize, optimize, and activate enzymes, as well as localize proteins to specific organelles and membranes. Glycosyltransferases-enzymes that attach sugars to polysaccharides, proteins, lipids, and RNA-across multiple plant biosynthetic processes have been demonstrated to interact with one another. The mechanisms behind these interactions are still unknown, but recent research has highlighted extensive examples of protein-protein interactions, specifically in the plant cell wall hemicellulose and pectin biosynthesis that takes place in the Golgi apparatus. In this review, we will discuss what is known so far about the interactions among Golgi-localized glycosyltransferases that are important for their functioning, trafficking, as well as structural aspects.
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