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Nature Cell Biology  6, 379 - 380 (2004)
doi:10.1038/ncb0504-379

N-terminal acetylation targets GTPases to membranes

Catherine L. Jackson

Catherine L. Jackson is in the Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA. cathyj@helix.nih.gov

The small GTPases Arl3p and Arl1p function sequentially to recruit diverse effector proteins to the Golgi apparatus. Similarly to ARF proteins, Arl1p is targeted to membranes by myristoylation. Arl3p, however, is not myristoylated. Recent work demonstrates that Arl3p, and its mammalian orthologue ARFRP1, are targeted to membranes by amino-terminal acetylation, which facilitates recognition by the membrane receptor Sys1p/hSys1.

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Cell biology GTPase traffic control

Nature News and Views (15 Jun 2000)

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Nature Cell Biology
ISSN: 1465-7392
EISSN: 1476-4679
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