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The cytoplasmic and transmembrane domains of secretor type α 1,2fucosyltransferase confer atypical cellular localisation
Author(s) -
Christiansen Dale,
Milland Julie,
Dodson Hayley C.,
Lazarus Brooke D.,
Sandrin Mauro S.
Publication year - 2009
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/jmr.939
Subject(s) - golgi apparatus , cytoplasm , biology , transmembrane protein , biochemistry , amino acid , enzyme , peptide sequence , epitope , microbiology and biotechnology , cell , antibody , gene , genetics , receptor
Carbohydrate structures influence many aspects of cell biology. Manipulating the glycosyltransferase enzymes, that sequentially add carbohydrate moieties to proteins and lipids as they pass through the Golgi and secretory pathway, can alter these carbohydrate epitopes. We previously demonstrated that the eight amino acid cytoplasmic tail of α 1,2fucosyltransferase (FT) contained a sequence for Golgi localisation. In this study, we examined the localisation of the closely related secretor type α 1,2fucosyltransferase (Sec) which has a smaller, yet apparently unrelated, five amino acid cytoplasmic tail. In contrast to the Golgi localisation of FT, Sec displayed atypical cytoplasmic vesicular‐like staining. However, replacing just the five amino acid tail of Sec with FT was sufficient to relocalise the enzyme to a perinuclear region with Golgi ‐ like staining. The biological significance of this relocalisation was this chimaeric enzyme was more effective than FT at competing for N‐Acetyl‐lactosamine and thus was superior in reducing expression of the Gal α (1,3)Gal xenoepitope. Copyright © 2009 John Wiley & Sons, Ltd.