REGULATION OF CYTOPLASMIC DYNEIN BASED VESICLE TRANSPORT

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 动力蛋白是一种多亚基蛋白复合物，与微管马达细胞质动力蛋白协同作用，提供广泛的亚细胞定位和运动功能。Dynactin通过增强运动持续合成能力和作为衔接蛋白使动力蛋白与各种亚细胞货物相互作用来辅助动力蛋白。 为了做到这一点，动力蛋白依赖于其结构的不同元素的独特结合活性。 货物结合域和动力蛋白结合域允许动力蛋白作为动力蛋白适配器，而持续合成能力的增强取决于微管结合域和动力蛋白结合域。所有已知的基于细胞质动力蛋白的转运都需要动力蛋白的结构完整性。 动力蛋白亚基动力蛋白（p50）作为一种分子“胶”，将动力蛋白和动力蛋白的微管结合亚基p150（Glued）锚定在货物结合元件上。在动力肌动蛋白中，动力蛋白与至少三个其他动力肌动蛋白亚基以及自身接触。 该项目的重点是获得新的信息dynactin亚基组织，dynactin亚基的修饰，并确定与dynactin在细胞中相互作用的蛋白质。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Dynactin is a multisubunit protein complex that works in conjunction with the microtubule-based motor, cytoplasmic dynein, to provide a wide range of subcellular localization and motile functions. Dynactin assists dynein by enhancing motor processivity and serving as an adaptor protein that allows dynein to interact with a variety of subcellular cargoes. To do this, dynactin relies on the distinct binding activities of different elements of its structure. The cargo-binding and dynein-binding domains allow dynactin to serve as a dynein adaptor, while processivity enhancement depends on the microtubule-binding and dynein-binding domains. All known cytoplasmic dynein-based transport requires dynactin's structural integrity. The dynactin subunit dynamitin (p50) acts as a molecular "glue" that anchors the dynein and microtubule-binding subunit of dynactin, p150(Glued), to the cargo-binding element. Within dynactin, dynamitin makes contacts with at least three other dynactin subunits as well as itself. This project is focused on obtaining new information on dynactin subunit organization, modification of dynactin subunits, and identifying proteins with which dynactin interacts in cells.