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N-糖基化在上皮细胞顶端膜蛋白转运中的作用。

Role of N-glycosylation in trafficking of apical membrane proteins in epithelia.

作者信息

Vagin Olga, Kraut Jeffrey A, Sachs George

机构信息

Department of Physiology, David Geffen School of Medicine at University of California, Bldg. 113, Rm. 324, 11301 Wilshire Blvd., Los Angeles, California 90073, USA.

出版信息

Am J Physiol Renal Physiol. 2009 Mar;296(3):F459-69. doi: 10.1152/ajprenal.90340.2008. Epub 2008 Oct 29.

Abstract

Polarized distribution of plasma membrane transporters and receptors in epithelia is essential for vectorial functions of epithelia. This polarity is maintained by sorting of membrane proteins into apical or basolateral transport containers in the trans-Golgi network and/or endosomes followed by their delivery to the appropriate plasma membrane domains. Sorting depends on the recognition of sorting signals in proteins by specific sorting machinery. In the present review, we summarize experimental evidence for and against the hypothesis that N-glycans attached to the membrane proteins can act as apical sorting signals. Furthermore, we discuss the roles of N-glycans in the apical sorting event per se and their contribution to folding and quality control of glycoproteins in the endoplasmic reticulum or retention of glycoproteins in the plasma membrane. Finally, we review existing hypotheses on the mechanism of apical sorting and discuss the potential roles of the lectins, VIP36 and galectin-3, as putative apical sorting receptors.

摘要

上皮细胞中质膜转运蛋白和受体的极化分布对于上皮细胞的向量功能至关重要。这种极性通过在反式高尔基体网络和/或内体中将膜蛋白分选到顶端或基底外侧运输容器中,随后将它们递送到适当的质膜结构域来维持。分选取决于特定分选机制对蛋白质中分选信号的识别。在本综述中,我们总结了支持和反对膜蛋白上连接的N-聚糖可作为顶端分选信号这一假说的实验证据。此外,我们讨论了N-聚糖在顶端分选事件本身中的作用,以及它们对内质网中糖蛋白折叠和质量控制或糖蛋白在质膜中保留的贡献。最后,我们综述了关于顶端分选机制的现有假说,并讨论了凝集素VIP36和半乳糖凝集素-3作为假定的顶端分选受体的潜在作用。

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