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GCC185, a trans-Golgi network-localized protein predicted to assume a long, coiled-coil structure, is required for Rab9-dependent recycling of mannose 6-phosphate receptors (MPRs) to the Golgi and for microtubule nucleation at the Golgi via CLASP proteins. GCC185 localizes to the Golgi by cooperative interaction with Rab6 and Arl1 GTPases at adjacent sites… (More)
Enzymes called Rab GTPases that carry so-called "activating" mutations may never become activated at all.
TRAPPI is a multisubunit protein complex on the Golgi that activates the small GTPase Ypt1p to facilitate the receipt of transport vesicles inbound from the endoplasmic reticulum. Cai et al. (2008) now present structural and biochemical analyses of yeast TRAPPI in a complex with Ypt1p revealing a unique mechanism by which TRAPPI catalyzes guanine nucleotide… (More)