期刊
MOLECULAR BIOLOGY OF THE CELL
卷 14, 期 12, 页码 5089-5097出版社
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E03-01-0025
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资金
- NIDDK NIH HHS [DK-44375] Funding Source: Medline
- NIGMS NIH HHS [GM-44589, R56 GM044589, R01 GM044589] Funding Source: Medline
- NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES [P01DK044375] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R56GM044589, R01GM044589] Funding Source: NIH RePORTER
Cytoplasmic dynein and dynactin are megadalton-sized multisubunit molecules that function together as a cytoskeletal motor. In the present study, we explore the mechanism of dynein-dynactin binding in vitro and then extend our findings to an in vivo context. Solution binding assays were used to define binding domains in the dynein intermediate chain (IC) and dynactin p150(Glued) subunit. Transient overexpression of a series of fragments of the dynein IC was used to determine the importance of this subunit for dynein function in mammalian tissue culture cells. Our results suggest that a functional dynein-dynactin interaction is required for proper microtubule organization and for the transport and localization of centrosomal components and endomembrane compartments. The dynein IC fragments have different effects on endomembrane localization, suggesting that different endomembranes may bind dynein via distinct mechanisms.
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