Association of -1,3-N-acetylglucosaminyltransferase 1 and -1,4-galactosyltransferase 1, trans-Golgi enzymes involved in coupled poly-N-acetyllactosamine synthesis

Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305, USA.
Glycobiology (Impact Factor: 3.15). 04/2009; 19(6):655-64. DOI: 10.1093/glycob/cwp035
Source: PubMed


Poly-N-acetyllactosamine (polyLacNAc) is a linear carbohydrate polymer composed of alternating N-acetylglucosamine and galactose residues involved in cellular functions ranging from differentiation to metastasis. PolyLacNAc
also serves as a scaffold on which other oligosaccharides such as sialyl Lewis X are displayed. The polymerization of the
alternating N-acetylglucosamine and galactose residues is catalyzed by the successive action of UDP-GlcNAc:βGal β-1,3-N-acetylglucosaminyltransferase 1 (B3GNT1) and UDP-Gal:βGlcNAc β-1,4-galactosyltransferase, polypeptide 1 (B4GALT1), respectively.
The functional association between these two glycosyltransferases led us to investigate whether the enzymes also associate
physically. We show that B3GNT1 and B4GALT1 colocalize by immunofluorescence microscopy, interact by coimmunoprecipitation,
and affect each other's subcellular localization when one of the two proteins is artificially retained in the endoplasmic
reticulum. These results demonstrate that B3GNT1 and B4GALT1 physically associate in vitro and in cultured cells, providing
insight into possible mechanisms for regulation of polyLacNAc production.

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    • "We transfected HPAC cells with RFP-taged B4GALT1 as a TGN marker. It was shown that B4GALT1 is mainly located in the TGN, and for some extent, medial Golgi [12]. B4GALT1-transfected HPAC cells were serum-starvated for 48 hours and 7 nM TGF-α was added for 30 min. "
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