Interaction with Gβγ Is Required for Membrane Targeting and Palmitoylation of Gαs and Gαq *

By D. Evanko, M. Thiyagarajan, P. Wedegaertner. Journal of Biological Chemistry, 2000

114 citations recorded by the source corpus.

Peripheral membrane proteins utilize a variety of mechanisms to attach tightly, and often reversibly, to cellular membranes. The covalent lipid modifications, myristoylation and palmitoylation, are critical for plasma membrane localization of heterotrimeric G protein α subunits. For αs and αq, two subunits that are palmitoylated but not myristoylated, we examined the importance of interacting with the G protein βγ dimer for their proper plasma membrane localization and palmitoylation. Conserved α subunit N-terminal amino acids predicted to mediate binding to βγ were mutated to create a series of βγ binding region mutants expressed in HEK293 cells. These αs and αq mutants were found in soluble rather than particulate fractions, and they no longer localized to plasma membranes as demonstrated by immunofluorescence microscopy. The mutations also inhibited incorporation of radiolabeled palmitate into the proteins and abrogated their signaling ability. Additional αq mutants, which contain these mutations but are modified by both myristate and palmitate, retained their localization to plasma membranes and ability to undergo palmitoylation. These findings identify binding to βγ as a critical membrane attachment signal for αs and αq and as a prerequisite for their palmitoylation, while myristoylation can restore membrane localization and palmitoylation of βγ binding-deficient αq subunits.

Subfields: Immunology and Allergy, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/1f61db10cdd5895f8918a0ded21dd4db8dcf88dc

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Citations in the corpus

Heterotrimeric G Protein γ Subunits Provide Functional Selectivity in Gβγ Dimer Signaling in Arabidopsis[OA] (2007, background): “Aside from the activation of specific downstream effectors, the Gbg dimer is involved in receptor recognition (Lim et al., 2001), membrane targeting, and activation of the Ga subunit (Evanko et al., 2000, 2001).”