Regulation of the processivity and intracellular localization of Saccharomyces cerevisiae dynein by dynactin.

摘要: Dynactin, a large multisubunit complex, is required for intracellular transport by dynein; however, its cellular functions and mechanism of action are not clear. Prior studies suggested that dynactin increases dynein processivity tethering the motor to microtubule through own binding domains. However, this hypothesis could be tested without recombinant source dynactin. Here, we have produced in Saccharomyces cerevisiae, examined effect on single-molecule motility assays. We show run length single motors, but does alter directionality movement. Enhancement require (MT) domains Nip100 (the yeast p150Glued homolog). Dynactin lacking these MT also supports proper localization function during nuclear segregation vivo. Instead, segment coiled-coil activities. Our results directly demonstrate independent tethering.