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© Research
Publication : Neurochemical research

Spatial organization and stoichiometry of N-terminal domain-mediated glycosyltransferase complexes in Golgi membranes determined by fret microscopy.

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Neurochemical research - 01 Jun 2012

Ferrari ML, Gomez GA, Maccioni HJ,

Link to Pubmed [PMID] – 22388569

Link to DOI – 10.1007/s11064-012-0741-1

Neurochem Res 2012 Jun; 37(6): 1325-34

The functional link between glycolipid glycosyltransferases (GT) relies on the ability of these proteins to form organized molecular complexes. The organization, stoichiometry and composition of these complexes may impact their sorting properties, sub-Golgi localization, and may determine relative efficiency of GT in different glycolipid biosynthetic pathways. In this work, by using Förster resonance energy transfer microscopy in live CHO-K1 cells, we investigated homo- and hetero-complex formation by different GT as well as their spatial organization and molecular stoichiometry on Golgi membranes. We find that GalNAcT and GalT2 Ntd are able to form hetero-complexes in a 1:2 molar ratio at the trans-Golgi network and that GalT2 but not GalNAcT forms homo-complexes. Also, GalNAcT/GalT2 complexes exhibit a stable behavior reflected by its clustered lateral organization. These results reveals that particular topological organization of GTs may have functional implications in determining the composition of glycolipids in cellular membranes.

https://pubmed.ncbi.nlm.nih.gov/22388569