Table 6. Ability of GFP-tagged stomatin mutants to target the plasma membrane, form oligomers, and/or associate with DRMs.

Mutation	Affected domain	PM localization	Oligo-merization	DRM-association
WT	─	+	+	+
ΔN	N-terminal	+	+	+
ΔC	C-terminal	+	-	-
ΔCC	Coiled-coil	+	-	+
Cys30Ser	IM	+	+	+
Pro47Ser	IM	-	-	-
Ile57Ala	CRAC/CARC	(+)	+	+
Tyr60Ala	CRAC/CARC	(+)	-	-
Arg62Ala	CRAC/CARC	+	-	-
Cys87Ser	PHB/SPFH	-	(+)	+
Phe91Ala	PHB/SPFH	+	(+)*	-
Arg97Ala	PHB/SPFH	-	-	+
Pro200Ala	Coiled-coil	(+)	-	+
Pro245Ala	Coiled-coil	(+)	-	(+)
Phe269Ala	ORA/CARC	+	-	+
Pro270Ala	ORA/CARC	-	-	+

PM, plasma membrane; DRM, detergent-resistant membrane; WT, wildtype; ΔN, N-terminal deletion; ΔC, C-terminal deletion; ΔCC, coiled-coil deletion; IM, intramembrane domain; CRAC, cholesterol recognition/interaction amino acid consensus sequence; CARC, reverse CRAC motif; PHB, prohibitin homology domain; SPFH, stomatin-prohibitin-flotillin-HflK/C domain; ORA, oligomerization and lipid raft association domain; +, positive; -, negative; (+), lower than WT; (+)* denotes the unclear condition of Phe91Ala oligomers, which rather appear like unspecific aggregates (Fig 3, left panel; Table 2).