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Please use this identifier to cite or link to this item: http://hdl.handle.net/1807/25554

Title: Defining the Mechanisms by which Palmitoylation Regulates the Localization and Function of RGS4
Authors: Dissanayake, Kaveesh
Advisor: Heximer, Scott P.
Department: Physiology
Keywords: RGS4
G protein
plasma membrane
Issue Date: 31-Dec-2010
Abstract: Regulator of G-protein signalling 4 (RGS4) modulates Gq and Gi signalling at the plasma membrane (PM). It has been demonstrated that the addition of palmitate to cysteine residues is an important regulator of RGS protein localization and function. The family of palmitate transferase enzymes shares a conserved Asp-His-His-Cys (DHHC) motif. We set out to establish the DHHC isoform(s) that affect RGS4 activity in HEK201 cells. Confocal microscopy revealed that overexpression of DHHCs 3 and 7 mobilized RGS4 to the Golgi. Knockdown of either DHHC3 or DHHC7 attenuated RGS4 inhibition of Gαq-coupled Ca2+ release and reduced RGS4 PM localization. Consistent with a role in promoting RGS4 lipid bilayer targeting, dominant negative mutants of the five most highly expressed DHHCs in HEK201 cells also diminished RGS4 PM association. Together, these data suggest that members of the mammalian DHHC family regulate RGS4 localization and function, likely through palmitoylation of its target cysteine residues.
URI: http://hdl.handle.net/1807/25554
Appears in Collections:Master
Department of Physiology - Master theses

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