Beck K A, Nelson W J
Department of Cell Biology and Human Anatomy, School of Medicine, University of California, Davis, CA 95616, USA.
Biochim Biophys Acta. 1998 Aug 14;1404(1-2):153-60. doi: 10.1016/s0167-4889(98)00054-8.
The existence of a Golgi-localized membrane cytoskeleton has been revealed by the identification of two major components of the spectrin membrane skeleton, spectrin and ankyrin, that associate with the Golgi complex. Golgi spectrin was identified with an antibody specific for the beta-subunit of the erythroid isoform of spectrin (beta1Sigma1). This antibody recognizes a 220 kDa polypeptide that localizes to discrete regions of the Golgi complex and associates with Golgi membranes in a Brefeldin A sensitive manner. Two isoforms of Golgi ankyrin have been identified: a 119 kDa form (AnkG119) which represents a truncated, alternatively spliced isoform of a recently cloned novel ankyrin of the nervous system AnkG, and a larger 195 kDa ankyrin (Ank195) that cross-reacts with antibodies to erythrocyte ankyrin. A Golgi localized membrane skeleton composed of these unique membrane skeleton isoforms could serve a variety of important functions, including the maintenance of Golgi structural organization and the formation of discrete membrane domains within Golgi compartments.
通过鉴定血影蛋白膜骨架的两个主要成分血影蛋白和锚蛋白，它们与高尔基体复合物相关联，高尔基体定位的膜细胞骨架的存在得以揭示。用针对血影蛋白红细胞异构体β亚基（β1Sigma1）的特异性抗体鉴定了高尔基体血影蛋白。该抗体识别一种220 kDa的多肽，其定位于高尔基体复合物的离散区域，并以对布雷菲德菌素A敏感的方式与高尔基体膜相关联。已鉴定出两种高尔基体锚蛋白异构体：一种119 kDa的形式（AnkG119），它代表最近克隆的神经系统新型锚蛋白AnkG的截短、选择性剪接异构体，以及一种更大的195 kDa锚蛋白（Ank195），它与抗红细胞锚蛋白的抗体发生交叉反应。由这些独特的膜骨架异构体组成的高尔基体定位膜骨架可以发挥多种重要功能，包括维持高尔基体的结构组织以及在高尔基体区室内形成离散的膜结构域。
