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

被引:26
|
作者
Lee, Peter L. [1 ]
Kohler, Jennifer J. [2 ]
Pfeffer, Suzanne R. [1 ]
机构
[1] Stanford Univ, Dept Biochem, Sch Med, Stanford, CA 94305 USA
[2] Univ Texas SW Med Ctr Dallas, Div Translat Res, Dept Internal Med, Dallas, TX 75390 USA
基金
美国国家卫生研究院; 美国国家科学基金会;
关键词
endoplasmic reticulum; enzyme complexes; glycosyltransferase; Golgi complex; poly-N-acetyllactosamine; MEMBRANE-SPANNING DOMAIN; I-EXTENSION ENZYME; COMPLEX-FORMATION; SACCHAROMYCES-CEREVISIAE; ENDOPLASMIC-RETICULUM; TRANSMEMBRANE DOMAIN; RETENTION SIGNAL; CYTOPLASMIC TAIL; HEPARAN-SULFATE; KIN RECOGNITION;
D O I
10.1093/glycob/cwp035
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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:beta Gal beta-1,3-N-acetylglucosaminyltransferase 1 (B3GNT1) and UDP-Gal:beta GlcNAc beta-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.
引用
收藏
页码:655 / 664
页数:10
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