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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. Jackson1
- 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. e-mail: cathyj@helix.nih.gov
Abstract
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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