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. Author manuscript; available in PMC: 2008 May 5.
Published in final edited form as: J Neurosci. 2006 Dec 6;26(49):12758–12768. doi: 10.1523/JNEUROSCI.4214-06.2006

Figure 2.

Figure 2

Palmitoylation-dependent interaction of GODZ and SERZ-β with the γ2 subunit. The DHHC proteins FL-GODZ (a–c), FL-GODZC157S (d), or FL-SERZ-β (e, f) were cotransfected with YFPγ2(ICL) (a′, b′, d′–f′) or its mutant derivative YFPγ2(ICL)C3SA (c′) and tested for colocalization after treatment of transfected cells with ethanol (a–a″, e–e″) or 2-BrP in ethanol (b–b″, f–f″), or without additional treatment (c–c″, d–d″). Immunofluorescently labeled FL-GODZ and FL-SERZ-β are shown in red (a–f), the YFP-tagged γ2 constructs are shown in green (a′–f′), and colocalization of FL-GODZ or FL-SERZ-β with YFPγ2(ICL) is shown in yellow (a″–f″). Restriction of YFPγ2(ICL) to the Golgi is indicative of interaction with GODZ or SERZ-β. Note the diffuse distribution of YFP-tagged γ2 constructs in experiments involving transfection of GODZC157S (d) or YFPγ2(ICL)C3SA (c) or treatment with 2-BrP (b, f), respectively, indicating that palmitoylation is required for interaction between substrate and PATs.