The ability of epithelial cells to distinguish between domains on opposing cell surfaces within a tissue, a property known as planar cell polarity, relies on proteins and protein complexes directing the traffic of signaling proteins to specific locations on the cell surface membrane.

Mutations that reduce the functioning of rab7 may underlie the degeneration of sensory and motor nerves in Charcot-Marie-Tooth 2B disease, which suggests increasing endolysosomal function as a therapy.

Systems-level analysis in vertebrate ciliated epithelial cells shows that the network of genes activated by the transcription factor Rfx2 controls the development, migration, insertion and function of these cells.

Analysis of multiple guanine exchange factors shows that Rab activation can occur via a number of mechanistically distinct GDP-release pathways.

Asymmetric localization of the receptor EGFR within branches of axons is required to establish the precise wiring of neuronal networks within the Drosophila brain.

A small GTPase within the flagellum can participate in the control of transport from the base to the tip of the flagellum, and back again.

Centromeric protein M (CENP-M) is required for the stabilization of a quaternary complex that plays a crucial role in kinetochore organization and function.

The GEF activity of Rabex-5 is weakly autoinhibited by its CC domain and activated by Rabaptin-5 and the two proteins work concertedly to activate Rab5.

The dynein light intermediate chain is a member of the G protein superfamily and links the motor to several intracellular cargo adaptors.