The γ-subunit of the coatomer complex binds Cdc42 to mediate transformation

By W. J. Wu, J. Erickson, R. Lin, R. Cerione. Nature, 2000

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Bi-directional protein transport between the ER and Golgi. (2004, background): “Furthermore, γ - COP also binds to the Rho-related G protein, Cdc42, via a di-lysine motif, an interaction that may link vesicles to the actin cytoskeleton (Wu et al. 2000).”
Rho GTPases and cell migration. (2001, background): “This suggests that Cdc42 has another, or overlapping, function in regulating vesicle trafficking (Wu et al., 2000; Ridley, 2001).”
The α- and β′-COP WD40 Domains Mediate Cargo-selective Interactions with Distinct Di-lysine Motifs (2003, methodology): “Both photo-cross-linking data (Harter et al., 1996; Harter and Wieland, 1998) and in vitro binding data (Wu et al., 2000) have suggested that a binding site for di-lysine motifs is present on mammalian -COP.”
Differential Localization of Rho Gtpases in Live Cells (2001, background): “For example, the ER and Golgi localization of pCdc42hs is consistent with its ability to bind gCOP and regulate ER to Golgi transport (Wu et al., 2000).”
Cdc42 - the centre of polarity (2004, background): “Moreover, active Cdc42 binds directly to the coatomer complex and regulates vesicular trafficking between the endoplasmic reticulum and Golgi (Wu et al., 2000).”