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Making a raft with oligomers

The Journal of Cell Biology
The Rockefeller University Press
Publication Date
DOI: 10.1083/jcb1674iti5
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1674iti IN THIS ISSUE • THE JOURNAL OF CELL BIOLOGY 579 Text by Rabiya Tuma [email protected] Making a raft with oligomers pithelial cells differentially segregate pro- teins to their apical and basolateral surfaces. For some apical localization events, asso- ciation of glycosylphosphatidylinositol (GPI)- anchored proteins with detergent-resistant rafts is necessary but not sufficient. Now, on page 699, Paladino et al. show that the key for proper protein sorting may be the formation of high molecular weight aggregates of apically targeted GPI-anchored proteins as they segregate into rafts in the Golgi. The researchers separated rafts on sucrose gradients. The rafts containing apical proteins, like PLAP and GFP-GPI, had a high concentration of protein when compared with rafts with baso- laterally targeted proteins. Mutations of GFP-GPI that impaired formation of high molecular weight complexes caused mis-targeting of the protein to the basolateral surface. Using pulse-chase experi- ments, the researchers found that oligomerization occurred as the protein-laden rafts made their way through the trans-Golgi network. E Oligomerization may drive formation of apical vesicles. Invadolysin opens many doors n a search for proteins involved in chromo- some condensation, McHugh et al. (page 673) have identified a novel metalloprotease, IX- 14/invadolysin, that is required for both mitosis and cell motility in Drosophila , and probably also in human cells. The mutation, identified in a chemical muta- genesis screen, blocks cell proliferation as evidenced by underdeveloped brains and imaginal discs in larvae. It disrupts compaction of both interphase and mitotic chromosomes, such that mitotic chromo- somes are hypercondensed in length but with a loose peripheral halo of chromatin. The mutation also results in aberrant spindle assembly and in- I Invadolysin (green) localizes to structures resembling invadopodia. creased levels of some

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