UDP-N-acetylglucosamine transporter and UDP-galactose transporter form heterologous complexes in the Golgi membrane
UDP-N-acetylglucosamine transporter and UDP-galactose transporter form heterologous complexes in the Golgi membrane
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DOI：
10.1016/j.febslet.2012.10.016
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发表时间：
2012-11-30
期刊：
影响因子：
3.5
通讯作者：
Olczak, Mariusz
中科院分区：
文献类型：
--
作者：
Maszczak-Seneczko, Dorota;Sosicka, Paulina;Olczak, Mariusz
UDP-半乳糖转运蛋白(UGT；SLC35A2)和UDP-N-乙酰氨基葡萄糖转运蛋白(NGT；SLC35A3)在进化上是相关的。我们推测，它们在糖基化中的作用可能是通过形成异源复合体来耦合的。在活细胞上进行的免疫共沉淀分析和薄膜FRET测量表明，NGT和UGT在MDCK-RCAR细胞中过表达时形成复合体。我们还假设，NGT和UGT的相互作用可能解释了UGT2的双重定位。我们首次在体内证明了NGT核苷酸糖转运蛋白的同源二聚化。综上所述，我们认为NGT和UGT在糖基化中的功能是通过相互作用而结合在一起的。
UDP-galactose transporter (UGT; SLC35A2) and UDP-N-acetylglucosamine transporter (NGT; SLC35A3) are evolutionarily related. We hypothesize that their role in glycosylation may be coupled through heterologous complex formation. Coimmunoprecipitation analysis and FLIM-FRET measurements performed on living cells showed that NGT and UGT form complexes when overexpressed in MDCK-RCAr cells. We also postulate that the interaction of NGT and UGT may explain the dual localization of UGT2. For the first time we demonstrated in vivo homodimerization of the NGT nucleotide sugar transporter. In conclusion, we suggest that NGT and UGT function in glycosylation is combined via their mutual interaction.