z-logo
Premium
Recruitment of CG‐NAP to the Golgi apparatus through interaction with dynein–dynactin complex
Author(s) -
Kim HonSong,
Takahashi Mikiko,
Matsuo Kazuhiko,
Ono Yoshitaka
Publication year - 2007
Publication title -
genes to cells
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.912
H-Index - 115
eISSN - 1365-2443
pISSN - 1356-9597
DOI - 10.1111/j.1365-2443.2007.01055.x
Subject(s) - dynactin , dynein , microtubule , golgi apparatus , nap , microbiology and biotechnology , biology , protein subunit , cytoplasm , microtubule organizing center , dynein atpase , centrosome , biochemistry , cell , endoplasmic reticulum , neuroscience , gene , cell cycle
The structural organization and position of the Golgi apparatus are highly regulated by microtubule cytoskeleton and microtubule motor proteins. The mechanisms linking these proteins to the Golgi apparatus remain elusive. Here, we found that c entrosome and G olgi‐localized PK N a ssociated p rotein (CG‐NAP) was localized to the Golgi apparatus in a microtubule‐dependent manner. Microtubule‐binding experiments revealed that CG‐NAP possessed two microtubule‐binding domains. We also found that CG‐NAP was well co‐localized with cytoplasmic dynein subunits during recovery from the on‐ice treatment of cells that induced dissociation of CG‐NAP from the Golgi. Similar co‐localization was observed during recovery from the acetate treatment, which has been reported to inhibit the dynein‐mediated transport. CG‐NAP was co‐immunoprecipitated with a dynactin subunit p150 Glued . Expressing the p150 Glued ‐binding region of CG‐NAP fused with mitochondria‐targeting sequence induced recruitment of mitochondria to the pericentriolar area, suggesting that this region interacts with functional cytoplasmic dynein in vivo . Moreover, over‐expression of this region caused fragmentation of the Golgi similar to that of dynamitin. These results suggest that CG‐NAP is recruited to the minus ends of microtubules by interacting with cytoplasmic dynein, thereby localizes to the Golgi apparatus in a microtubule‐dependent manner and possibly involved in the formation of the Golgi near the centrosomes.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here