Brand S H, Castle J D
Department of Anatomy and Cell Biology, University of Virginia Health Sciences Center, Charlottesville 22908.
EMBO J. 1993 Oct;12(10):3753-61. doi: 10.1002/j.1460-2075.1993.tb06053.x.
Secretory carrier membrane proteins (SCAMPs) are widely distributed as components of post-Golgi membranes that function as recycling carriers to the cell surface. In fibroblasts, SCAMPs are concentrated in compartments involved in the endocytosis and recycling of cell surface receptors while in neurons and other cell types having regulated transport pathways, SCAMPs are also components of regulated carriers (synaptic vesicles, secretion granules and transporter vesicles). Their presence in multiple pathways distinguishes them from proteins (e.g. recycling cell surface receptors and synaptic vesicle proteins) which are concentrated in selected pathways. The SCAMPs also do not appear to reside beyond the boundaries of these pathways. This distribution suggests that SCAMPs are general markers of membranes that function in cell surface recycling. The primary sequence of SCAMP 37 reveals a novel polypeptide containing a series of structural motifs, including a calcium binding domain, a leucine zipper and two zinc fingers. The very broad tissue distribution, subcellular localization and sequence analysis all predict that SCAMPs play a fundamental role in cell surface recycling.
分泌载体膜蛋白(SCAMPs)作为高尔基体后膜的组成成分广泛分布,其功能是作为细胞表面的回收载体。在成纤维细胞中,SCAMPs集中在内吞作用和细胞表面受体回收所涉及的区室中,而在具有调节转运途径的神经元和其他细胞类型中,SCAMPs也是调节载体(突触小泡、分泌颗粒和转运小泡)的组成成分。它们在多种途径中的存在使其区别于集中在特定途径中的蛋白质(如回收细胞表面受体和突触小泡蛋白)。SCAMPs似乎也不存在于这些途径的边界之外。这种分布表明SCAMPs是细胞表面回收中发挥作用的膜的通用标记物。SCAMP 37的一级序列揭示了一种新型多肽,其包含一系列结构基序,包括一个钙结合结构域、一个亮氨酸拉链和两个锌指。非常广泛的组织分布、亚细胞定位和序列分析都预测SCAMPs在细胞表面回收中起基本作用。