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First published online September 7, 2006

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Arl1p drops GPI anchor at the membrane

Glycosylphosphatidylinositol (GPI) anchors tether various proteins to the plasma membrane. How such proteins are delivered from the trans-Golgi network (TGN) to the cell periphery is unclear. On p. 3845, Fang-Jen Lee and co-authors implicate the small Arf-like GTPase Arl1p in the process. Arl1p functions in the regulation of Golgi structure and in membrane trafficking at the TGN, but until now no Arl1p-regulated cargo had been identified. The authors show that the GPI-anchored yeast protein Gas1p, which normally resides at the cell surface, accumulates in internal structures in an arl1 mutant rather than moving to the plasma membrane. By contrast, they find that several cell-wall-localized GPI-anchored proteins and a non-GPI-anchored plasma membrane protein are transported normally in the arl1 mutant. Additional experiments indicate that the Arl1p regulators Sys1p and Arl3p, and its effector Imh1p, are also involved in Gas1p transport. Thus, the authors suggest, the Sys1p-Arl3p-Arl1p-Imh1p signalling cascade facilitates the transport of a subgroup of GPI-anchored proteins from the TGN to the plasma membrane.

Related articles in JCS:

Arl1p is involved in transport of the GPI-anchored protein Gas1p from the late Golgi to the plasma membrane

Ya-Wen Liu, Szu-Wei Lee, and Fang-Jen S. Lee
JCS 2006 119: 3845-3855. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content