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Compartmentalization of anaphase-promoting complexes

The anaphase-promoting complex (APC) promotes the ubiquitylation and destruction of cyclin B and other proteins during mitosis. It targets different substrates at different times, and degradation of a substrate can depend on its subcellular location. In syncytial Drosophila embryos, for example, only spindle-associated cyclin B is degraded. How this is achieved is far from clear — particularly given controversy over where APC itself resides. Jun-yong Huang and Jordan Raff have approached the problem by expressing GFP fusion proteins containing core APC subunits (Cdc27 and Cdc16) in syncytial fly embryos (see p. 2847). They find that, at mitosis, only a small fraction of cellular APC associates with the spindle. Global activation of spindle-restricted APC therefore cannot be responsible for cyclin B degradation; instead the cell must specifically activate an APC subpopulation. Huang and Raff also find that GFP-Cdc27 associates with mitotic chromosomes but GFP-Cdc16 does not; moreover, they show that RNAi-induced depletion of Cdc27 and Cdc16 produces distinct mitotic-arrest phenotypes. This suggests that cells produce multiple forms of APC, which are differentially localized and have distinct functions.

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Related articles in JCS:

The dynamic localisation of the Drosophila APC/C: evidence for the existence of multiple complexes that perform distinct functions and are differentially localised

Jun-yong Huang and Jordan W. Raff
JCS 2002 115: 2847-2856. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?