An MBoC favorite: Malectin: a novel carbohydrate-binding protein of the endoplasmic reticulum and a candidate player in the early steps of protein N-glycosylation.
An MBoC favorite: Malectin: a novel carbohydrate-binding protein of the endoplasmic reticulum and a candidate player in the early steps of protein N-glycosylation.
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DOI：
10.1091/mbc.e12-02-0156
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发表时间：
2012-06
影响因子：
3.3
通讯作者：
Hebert DN
中科院分区：
文献类型：
--
作者：
Hebert DN
N-连接聚糖最初作为三葡糖基化物质在内质网（ER）中转移，随后通过ER葡糖苷酶修剪其葡萄糖。凝集素分子伴侣钙连接蛋白和钙网蛋白与单糖基化聚糖侧链结合。在Schallus et al. 2008年，他填补了这一空白。本文对一种新发现的内质网糖结合蛋白malectin进行了全面的研究。碳水化合物微阵列分析被用来证明，malectin特异性结合二葡萄糖基化聚糖，和核磁共振结构研究暴露malectin的碳水化合物结合位点。鉴于其ER定位，malectin似乎定位于在早期分泌途径中辅助糖蛋白的成熟和质量控制中发挥重要作用。
N-linked glycans are originally transferred as triglucosylated species in the endoplasmic reticulum (ER) and then subsequently have their glucoses trimmed by ER glucosidases. The lectin molecular chaperones calnexin and calreticulin bind to monoglucosylated glycan side chains. No role had been ascribed to the diglucosylated species until the Schallus et al.(2008) article filled this void. In this paper, a comprehensive study of a newly identified ER carbohydrate-binding protein called malectin was performed. Carbohydrate microarray analysis was used to demonstrate that malectin specifically binds diglucosylated glycans, and nuclear magnetic resonance structural studies exposed the carbohydrate-binding site of malectin. In light of its ER localization, malectin appears to be positioned to play an important role in assisting the maturation and quality control of glycoproteins in the early secretory pathway.