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First published online 14 March 2006
doi: 10.1242/jcs.02958

Journal of Cell Science 119, 1494-1503 (2006)
Published by The Company of Biologists 2006
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Research Article

An N-terminally acetylated Arf-like GTPase is localised to lysosomes and affects their motility

Irmgard Hofmann and Sean Munro*

MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, UK

* Author for correspondence (e-mail: sean{at}mrc-lmb.cam.ac.uk)

Accepted 24 February 2006

Small GTPases of the Arf and Rab families play key roles in the function of subcellular organelles. Each GTPase is usually found on only one compartment and, hence, they confer organelle specificity to many intracellular processes. However, there has so far been little evidence for specific GTPases present on lysosomes. Here, we report that two closely related human Arf-like GTPases, Arl8a and Arl8b (also known as Arl10b/c and Gie1/2), localise to lysosomes in mammalian cells, with the single homologue in Drosophila cells having a similar location. Conventionally, membrane binding of Arf and Arl proteins is mediated by both an N-terminal myristoyl group and an N-terminal amphipathic helix that is inserted into the lipid bilayer upon activation of the GTPase. Arl8a and Arl8b do not have N-terminal myristoylation sites, and we find that Arl8b is instead N-terminally acetylated, and an acetylated methionine is necessary for its lysosomal localization. Overexpression of Arl8a or Arl8b results in a microtubule-dependent redistribution of lysosomes towards the cell periphery. Live cell imaging shows that lysosomes move more frequently both toward and away from the cell periphery, suggesting a role for Arl8a and Arl8b as positive regulators of lysosomal transport.

Key words: Arf family, GTPase, Lysosome, N-terminal acetylation


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