SGIP1 通过细胞内吞作用过程中 μHD 结构域内的分子间二硫键形成二聚体。
SGIP1 dimerizes via intermolecular disulfide bond in μHD domain during cellular endocytosis.
机构信息
State Key Laboratory of Medicinal Chemical Biology, Department of Biochemistry and Molecular Biology, College of Life Sciences, Nankai University, Tianjin, 300071, China.
State Key Laboratory of Medicinal Chemical Biology, Department of Biochemistry and Molecular Biology, College of Life Sciences, Nankai University, Tianjin, 300071, China.
出版信息
Biochem Biophys Res Commun. 2018 Oct 20;505(1):99-105. doi: 10.1016/j.bbrc.2018.09.075. Epub 2018 Sep 18.
Along with its homologs FCHo1 and FCHo2, SGIP1 plays an important role in clathrin-mediated endocytosis. The highly conserved C-terminal μHD domains in these proteins are the critical regions interacting with adapter molecules such as Eps15. The crystal structure of μHD domain of SGIP1 has been reported previously. In this study, we found that μHD domain of SGIP1 is capable of forming a stable dimer by an intermolecular disulfide bond formed by C632 in our crystal structure. The mutational study of C632 revealed that this residue is important for the function of SGIP1 during cellular endocytosis. Our study revealed a new dimerization and/or oligomerization manner in theses adaptor proteins, which is a critical prerequisite for their proper function.
与它的同源物 FCHo1 和 FCHo2 一样，SGIP1 在网格蛋白介导的内吞作用中发挥重要作用。这些蛋白质中高度保守的 C 末端 μHD 结构域是与衔接子分子（如 Eps15）相互作用的关键区域。SGIP1 μHD 结构域的晶体结构以前已有报道。在这项研究中，我们发现 SGIP1 的 μHD 结构域能够通过我们晶体结构中 C632 形成的分子间二硫键形成稳定的二聚体。C632 的突变研究表明，该残基对于 SGIP1 在细胞内吞作用过程中的功能很重要。我们的研究揭示了这些衔接子蛋白中的一种新的二聚化和/或寡聚化方式，这是其正常功能的关键前提。
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