. 2001 Nov;12(11):3601–3617. doi: 10.1091/mbc.12.11.3601

Table 1.

Colocalization of acylated proteins and lipid raft constituents in COS-7 cells

Protein	Membrane associating signals^a	Cellular localization^b	Colocalization^c with			Lipid raft association^d
Protein	Membrane associating signals^a	Cellular localization^b	Caveolin	Cholesterol	GM^a	Lipid raft association^d
YesGFP	myr⁺palm (3,5)^e	pm ⁺ endo	−	g⁺	h⁺	−
Yes(C3S)GFP	myr	endo ⁺ ER	−	⁺	⁺	−
Yes(G2A)GFP	none	cyto, nuc	−	−	−	−
FynGFP	myr⁺palm (3,6)	pm ⁺ endo	−	⁺	⁺	−
Gα_oGFP	myr⁺palm (3)	pm ⁺ endo	−	⁺	⁺	−
LckGFP	myr⁺palm (3,5)	pm ⁺ endo	−	⁺	⁺	−
Src₁₆GFP	myr⁺pos	pm ⁺ endo	−	⁺	⁺	−
GAP-43GFP	palm⁺pos (3,4)	pm ⁺ Golgi	⁺ (Golgi)	⁺	⁺	−
GFP	none	cyto, nuc	−	−	−	−
Caveolin	PTM⁺palm	pm/Golgi/ER/cyto^f	⁺	⁺^g	⁺^g	⁺
p62^c-yes	myr⁺palm	pm ⁺ endo^f	⁺	⁺^g	ND^h	⁺

Known cooperative signals responsible for membrane association. myr, myristoylation; pal, palmitoylation; pos, polybasic region; PTM, partial transmembrane domain.

As determined in this and a previous study (McCabe and Berthiaume, 1999). pm, plasma membrane; endo, endosomes; ER, endoplasmic reticulum; cyto, cytoplasm; Golgi, Golgi region.

Immunofluorescence using anti-GFP and anti-caveolin Abs. Cholesterol: free cholesterol as detected by filipin; GM₁, ganglioside GM₁ detection utilizing FITC-cholera toxin B subunit.

Lipid raft association as defined by 1% TX-100 and sodium carbonate sucrose gradient fractionation methods.

Numbers between parentheses refer to the position of palmitoylated cysteines.

As determined in Anderson (1998), Uittenbogaard et al. (1998), Luetterforst et al. (1999), and Luton et al. (1999).

Weak colocalization noted.

ND, Not determined.