位于高尔基体系统顺式-中间部分和反式部分的两种整合膜蛋白获得了唾液酸化的N-连接碳水化合物，并表现出不同的周转率和对cAMP依赖性磷酸化的敏感性。
Two integral membrane proteins located in the cis-middle and trans-part of the Golgi system acquire sialylated N-linked carbohydrates and display different turnovers and sensitivity to cAMP-dependent phosphorylation.
作者信息
Yuan L, Barriocanal J G, Bonifacino J S, Sandoval I V
出版信息
J Cell Biol. 1987 Jul;105(1):215-27. doi: 10.1083/jcb.105.1.215.
Abstract
The localization and chemical characteristics of two Golgi integral membrane proteins (GIMPs) have been studied using monoclonal antibodies. The two proteins are segregated in different parts of the Golgi system and whereas GIMPc(130 kD) is located in the cis and medial cisternae, GIMPt (100 kD) is confined in the trans-most cisterna and trans-tubular network. Both GIMPs are glycoproteins that contain N- and O-linked carbohydrates. The N-linked carbohydrates were exclusively of the complex type. Although excluded from the trans-side of the Golgi system, where sialylation is believed to occur, GIMPc acquires sialic acid in both its N- and O-linked carbohydrates. Sialic acid was also detected in the N-linked carbohydrates of GIMPt. GIMPc is apparently phosphorylated in the luminal domain in vivo. Phosphorylation occurred exclusively on serine and was stimulated by dibutyryl cyclic AMP. GIMPc and GIMPt displayed half-lives of 20 and 9 h, respectively.
摘要
利用单克隆抗体对两种高尔基体整合膜蛋白（GIMPs）的定位和化学特性进行了研究。这两种蛋白分布于高尔基体系统的不同部位，GIMPc（130kD）位于顺面和中间潴泡，而GIMPt（100kD）局限于最反面的潴泡和反式管状网络。两种GIMPs均为糖蛋白，含有N-连接和O-连接的碳水化合物。N-连接的碳水化合物均为复合型。尽管GIMPc被排除在高尔基体系统中据信发生唾液酸化的反面，但它的N-连接和O-连接碳水化合物中均获得了唾液酸。在GIMPt的N-连接碳水化合物中也检测到了唾液酸。GIMPc在体内管腔结构域明显发生磷酸化。磷酸化仅发生在丝氨酸上，并受二丁酰环磷腺苷刺激。GIMPc和GIMPt的半衰期分别为20小时和9小时。
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