title: Membrane targeting: getting Arl to the Golgi.
abstract: Post-translational modification with myristoyl or prenyl groups is essential for membrane association of many small GTPases in the Ras superfamily. Two recent papers show that, rather than myristoylation, amino-terminal acetylation of the Arf-like protein Arl3p is required for Golgi targeting via an interaction with an integral membrane protein called Sys1.
authors.affiliation: Department of Biological Sciences, Vanderbilt University, Nashville, Tennessee 37235-1634, USA. tr.graham@vanderbilt.edu
authors.forename: Todd R
authors.initials: TR
authors.lastname: Graham
mesh_terms: D020727:ADP-Ribosylation Factors / Q000378:metabolism*; D000107:Acetylation; D006056:Golgi Apparatus / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism*; D008954:Models, Biological; D011499:Protein Processing, Post-Translational / Q000502:physiology*; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism*; D033921:Vesicular Transport Proteins; D018631:ras Proteins / Q000378:metabolism* / Q000502:physiology
chemical_list: D008565:Membrane Proteins; D029701:Saccharomyces cerevisiae Proteins; C444081:Sys1 protein, S cerevisiae; D033921:Vesicular Transport Proteins; D020727:ADP-Ribosylation Factors; C490249:ARL3 protein, S cerevisiae; D018631:ras Proteins