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Biochem Biophys Res Commun. 2002 Mar 1;291(3):494-500.

Possible implication of Golgi-nucleating function for the centrosome.

Author information

1
Animal and Cellular Systems Laboratory, RIKEN (The Institute of Physical and Chemical Research), Hirosawa 2-1, Wako-shi, Saitama, 351-0198, Japan. atak@postman.riken.go.jp

Abstract

The Golgi apparatus breaks down at mitosis, resulting in the dispersal of Golgi-resident proteins. In NRK cells, however, subsets of both TGN38 and golgin-97, but not ManII and GM130, remained associated with the centrosome throughout the cell cycle. This centrosome association of TGN38 and golgin-97 was not disrupted by treatment with brefeldin A, additional inducers of retrograde trafficking and inhibitors of either kinases or protein phosphatases. Anchoring of the Golgi apparatus within the juxtanuclear region depends on microtubules; the association of TGN38 and golgin-97 subsets with the centrosome, however, was insensitive to nocodazole treatment. Drugs such as PDMP, which block Golgi dispersal both by nocodazole, despite microtubule depolymerization, and by inducers of retrograde trafficking, strengthened the microtubule-nucleating activity of the centrosome. These observations cumulatively suggest the centrosome is implicated in nucleation of the Golgi apparatus through interactions with Golgi-resident proteins, such as TGN38 and golgin-97.

PMID:
11855815
DOI:
10.1006/bbrc.2002.6433
[Indexed for MEDLINE]
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