Investigation of characteristics of zinc transporter ZIP13 protein

锌转运蛋白ZIP13在骨、牙齿和结缔组织发育中起着关键作用，其功能障碍导致了一种新型的Ehler-Danlos综合征：脊柱绒毛异常增殖型Ehler-Danlos综合征(SCD-EDS)。我们研究了人类野生型ZIP13蛋白的特性，以及由突变的ZIP13蛋白引起的SCD-EDS的致病机制。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)，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)。我们的发现表明，ZIP13野生型和突变型ZIP13蛋白可能与其生理病理机制有关。

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.