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Confocal images of Drosophila larval brains mutant for dynein. Microtubules are shown in red, DNA in green and CP190 in blue. Background confocal images are from Drosophila embryos with Dynamitin shown in green. Cover design: Lawrence Keogh
Commuters can ride a high-speed mass-transit system from the city centre to the suburbs and then engage a private vehicle for the final leg home. Similarly, vaccinia virions travel to the cell periphery on microtubule tracks, disembark near the plasma membrane, and acquire individual actin tails for propulsion on microvilli towards adjacent cells.
An ever-expanding and diverse collection of proteins and small molecules is involved in the pathways leading to protein disulphide bond formation. However, the origin of oxidative power for this process in the eukaryotic endoplasmic reticulum has remained mysterious. It has now been shown that in the yeast endoplasmic reticulum (ER), the catalyst Erv2p, a member of the Erv1p/ALR protein family, uses molecular oxygen directly to contribute oxidizing equivalents for disulphide bond formation.
Cell proliferation is regulated by temporal changes in gene expression in response to specific chemical and physical cues. These signals are relayed by a variety of intracellular signalling pathways including those activated by small GTPases, such as Ras, Rho, Rac and Cdc42. In this issue, Assoian and colleagues show that Rho confines the expression of cyclin D1 to mid-G1 phase of the cell cycle, by interactions with the ERK and Rac/Cdc42 signalling pathways.