EHD proteins are associated with tubular and vesicular compartments and interact with specific phospholipids
EHD proteins are associated with tubular and vesicular compartments and interact with specific phospholipids
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DOI：
10.1016/j.yexcr.2006.10.006
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发表时间：
2007-01-15
影响因子：
3.7
通讯作者：
Plomann, Markus
中科院分区：
文献类型：
--
作者：
Blume, Jessica J.;Halbach, Arndt;Plomann, Markus
四种包含 Eps15 同源 (EH) 结构域的蛋白 EHDI-EHD4 最近被认为在调节不同受体分子的循环中发挥作用，并且经常被发现与管状结构相关。在这里，我们报告了所有四种 EHD 蛋白在组织分布、细胞内定位和脂质结合特性方面的分析。特异性抗体揭示了组织和细胞内位置中各个蛋白质的不同表达谱，它们可能与特定的磷脂相互作用。此外，EHD 蛋白与囊泡和管状结构共定位，这意味着在运输过程和细胞骨架动力学中发挥作用。 N 端核苷酸结合 P 环区域携带突变的蛋白质变体不再与磷脂或膜区室相关，而 C 端 EH 结构域的删除会影响对管状结构的靶向。所有 EHD 蛋白都能够与磷脂结合，但每种蛋白的定位不同。 (c) 2006 Elsevier Inc. 保留所有权利。
The four Eps15 homology (EH) domain-containing proteins, EHDI-EHD4, have recently been ascribed roles in the regulation of the recycling of distinct receptor molecules and are often found associated with tubular structures. Here, we report the analysis of all four EHD proteins with regard to tissue distribution, intracellular localization and lipid binding properties. Specific antibodies reveal distinct expression profiles for the individual proteins in tissues and at intracellular locations, where they potentially interact with specific phospholipids. Moreover, EHD proteins colocalize with vesicular and tubular structures, implying roles in transport processes and cytoskeletal dynamics. Protein variants carrying mutations in the N-terminal nucleotide-binding P-loop region are no longer associated with phospholipids or membrane compartments, while deletion of the C-terminal EH domain affects targeting to tubular structures. All EHD proteins are able to bind to phospholipids, but localizations differ for each protein. (c) 2006 Elsevier Inc. All rights reserved.