Blume Jessica J, Halbach Arndt, Behrendt Dieter, Paulsson Mats, Plomann Markus
Center for Biochemistry and Center for Molecular Medicine, Medical Faculty, University of Cologne, Joseph-Stelzmann-Str 52, D-50931 Cologne, Germany.
Exp Cell Res. 2007 Jan 15;313(2):219-31. doi: 10.1016/j.yexcr.2006.10.006. Epub 2006 Oct 13.
The four Eps15 homology (EH) domain-containing proteins, EHD1-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.
四种含Eps15同源（EH）结构域的蛋白EHD1 - EHD4，最近被认为在不同受体分子的循环利用调节中发挥作用，并且常与管状结构相关联。在此，我们报告了对所有四种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。特异性抗体揭示了各蛋白在组织和细胞内位置的不同表达谱，在这些位置它们可能与特定磷脂相互作用。此外，EHD蛋白与囊泡和管状结构共定位，暗示其在运输过程和细胞骨架动力学中的作用。在N端核苷酸结合P环区域携带突变的蛋白变体不再与磷脂或膜区室相关联，而C端EH结构域的缺失影响靶向管状结构。所有EHD蛋白都能够结合磷脂，但每种蛋白的定位不同。
