Characterization of MDGA1, a novel human glycosylphosphatidylinositol-anchored protein localized in lipid rafts
Characterization of MDGA1, a novel human glycosylphosphatidylinositol-anchored protein localized in lipid rafts
复制标题
DOI：
10.1016/j.yexcr.2005.02.016
复制
发表时间：
2005-07-01
影响因子：
3.7
通讯作者：
De Juan, C
中科院分区：
文献类型：
--
作者：
Díaz-López, A;Rivas, C;De Juan, C
我们报道了由MDGA1（含糖基磷脂酰肌醇锚定-1的MAM结构域）基因编码的新型人类蛋白MDGA1的特征，该基因首次被绑定为GPIM。MDGA1已被定位到6p21，它在非人组织和肿瘤中表达。推导出的多肽由955个氨基酸组成，具有不同类型的细胞粘附分子（CAMs）的结构特征，例如免疫球蛋白结构域和MAM结构域的存在，或者通过GPI（糖基磷脂酰肌醇）基体锚定在细胞膜上的能力。我们的研究结果表明，人MDGA1 （hMDGA1）定位于真核细胞的细胞膜。该蛋白遵循分泌途径，最终通过GPI锚定保留在细胞膜内，易被磷脂酶C （PI-PLC）切割。此外，我们的研究结果表明hMDGA1特异性定位于称为脂筏的膜微域。最后，与分泌通路的其他蛋白一样，hMDGA1还经历了其他翻译后修饰，包括n -糖基化。(c) 2005爱思唯尔公司版权所有。
We report the characterization of the novel human protein MDGA1 encoded by MDGA1 (MAM domain containing glycosylphosphatidyl-inositol anchor-1) gene, firstly ten tied as GPIM.MDGA1 has been mapped to 6p21 and it is expressed inhuman tissues andturnors. The deduced polypeptide consists of 955 amino acids and exhibits structural features found in different types of cell adhesion molecules (CAMs), such as the presence of both immunoglobulin domains and a MAM domain or the capacity to anchor to the cell membrane by a GPI (glycosylphosphatidylinositol) motif. Our results demonstrate that human MDGA1 (hMDGA1) is localized in the membrane of eukaryotic cells. The protein follows the secretion pathway and finally it is retained in the cell membrane by a GPI anchor, susceptible to be cleavaged by phospholipase C (PI-PLC). Moreover, our results reveal that hMDGA1 is localized specifically into membrane microdomains known as lipid rafts. Finally, as other proteins of the secretory pathway, hMDGA1 undergoes other post-translational modification consisting of N-glycosylation. (c) 2005 Elsevier Inc. All rights reserved.