Investigation of characteristics of zinc transporter ZIP13 protein

锌转运蛋白ZIP13在骨骼、牙齿和结缔组织发育中起着至关重要的作用，其功能障碍是新型ehers - danlos综合征：脊椎发育不良形式的ehers - danlos综合征（SCD-EDS）的原因。我们研究了人类野生型ZIP13蛋白的特点，以及突变型ZIP13蛋白引起SCD-EDS的发病机制。我们发现ZIP13蛋白定位于高尔基体并形成同源二聚体状态（Bin, JBC 2011），并且突变的ZIP13蛋白通过蛋白酶体途径降解，导致细胞内锌稳态失衡（提交）。我们的发现提示了野生型和突变型ZIP13蛋白引发的生理病理机制。

The zinc transporter protein ZIP13 plays critical roles in bone, tooth, and connective tissue development, and its dysfunction is responsible for the novel type of Ehlers-Danlos syndrome: Spondylocheirodysplastic form of Ehlers-Danlos syndrome (SCD-EDS). We have investigated the characteristics of human wild-type ZIP13 protein, and the pathogenic mechanism of SCD-EDS caused by mutant ZIP13 proteins. We found that ZIP13 protein is localized to Golgi and forms homo-dimer state (Bin, JBC 2011), and mutant ZIP13 proteins are degraded by proteasome pathway leading to imbalanced intracellular Zn homeostasis (submitted). Our findings suggest that physio-pathological mechanisms elicited by wild-type and mutant ZIP13 proteins.