半桥粒是联结上皮细胞层与其它组织的重要结构，对维持人体组织结构稳定起到了不可缺少的作用。在细胞运动中，半桥粒与肌动蛋白细胞骨架的的动态联系保证了迁移能够正常进行，但其具体分子机制仍不清楚。秀丽线虫上皮细胞中的半桥粒无论结构还是蛋白组成都与哺乳动物高度近似，是研究半桥粒结构功能的理想模式。我们通过对线虫半桥粒的研究结果表明，半桥粒的动态重组与肌动蛋白骨架的重排过程高度协同。不仅如此，我们还发现了名为VAB-10B/BPAG1的半桥粒新组成蛋白，其哺乳动物同源基因为一种肌动蛋白结合蛋白。这些成果进一步拉近了半桥粒与肌动蛋白细胞骨架的关系。我们计划以VAB-10B为核心，深入探索半桥粒结构与细胞骨架的协同运作过程及其上游调控机制。其研究成果不但可以帮助解析多种半桥粒相关疾病的病理分子机制，更可帮助了解在细胞形态变化或运动过程中，半桥粒所代表的相对稳定的黏着结构与实时变化的细胞骨架间的普遍互动规律

Epithelial tissues form the architecture of most of our organs. Hemidesmosomes, being a crucial epidermal attachment structure, maintain tissue integrity and resistance to mechanical tension. During wound healing or carcinoma invasion, the interaction between hemidesmosomes and actin cytoskeleton is crucial for proper migration of epithelial cells. However, the underlying mechanisms for this interaction still remains elusive.?C.elegans hemidesmosomes (CeHDs) share similar structure and composition with their mammalian counterparts, making C. elegans an ideal model system for studying hemidesmosomes. We have recently discovered that CeHDs colocalize with actin bundles during late embryogenesis, and their reorganization processes are highly synchronized. In addition, we identified a novel CeHD component named VAB-10B/BPAG1, whose mammalian homolog is a classic actin-binding protein. These results further suggested a constant cross-talk between hemidesmosomes and actin cytoskeleton. We plan to take full advantage of C. elegans as an model organism, and explore the molecular mechanisms and regulation of hemidesmosome-actin interaction, mainly focusing on the characterization of the novel hemidesmosome protein VAB-10B. The results obtained from this study will not only extend our knowledge about the pathogenesis of various hemidesmosome-related diseases, but also provide insight into the generic rules of the interactions between relatively stable adhesion complexes and actively changing cytoskeletons.