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. 2011 Jun 1;22(11):1930–1942. doi: 10.1091/mbc.E10-10-0824

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© 2011 Levy et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).

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FIGURE 6: — A specific set of DHHC PATs promotes stathmin 2–4 palmitoylation. Individual HA-tagged DHHCs were cotransfected in HEK293 cells with either (A) myc-tagged full-length (St2-myc) or (B) the GFP-tagged A2 targeting domain (A2-GFP) of stathmin 2. After metabolic labeling with [³H]palmitic acid, proteins were separated by SDS–PAGE, and radioactive proteins were revealed by fluorography. Black dots indicate autopalmitoylation of expressed DHHC proteins. DHHC2, -3, -7, -15, and -21 enhanced the incorporation of [³H]palmitic acid into (A) St2 or (B) A2. (A) No signal was present when the two sites of palmitoylation of stathmin 2 were mutated into alanine (C22A/C24A). (B) Note that DHHC5 was also able to use A2-GFP as a substrate. (C) In HEK293 cells cotransfected with individual HA-tagged DHHCs and one of the GFP-tagged targeting A domain of stathmins 2–4 (A2, A3, and A4-GFP), the level of palmitoylation of the latter was estimated in comparison with that of full-length stathmin 2 as a reference: +++ for stathmin 2 palmitoylation by DHHC3 and -7; ++ by DHHC2; + by DHHC15 and -21; +/- by DHHC17; and – by DHHC5 and -16.