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. Author manuscript; available in PMC: 2011 Mar 1.
Published in final edited form as: Nature. 2010 Sep 2;467(7311):95–98. doi: 10.1038/nature09325

Figure 3. gSAP interacts with γ-secretase and APP-CTF but not with Notch.

Figure 3

a: Endogenous gSAP-16K in solubilized membrane preparations from N2a cells co-migrated with γ-secretase components during gel filtration (void volume: fraction 6). b: Immunoprecipitation of endogenous gSAP from N2a cells resulted in co-immunoprecipitation of γ-secretase components. c: Endogenous gSAP-16K and γ-secretase components are highly enriched by an immobilized γ-secretase transition state analogue (GSI beads). d: In HEK293 cells, gSAP-16K and APP-CTF, but not NotchΔE, co-immunoprecipitated. e: Imatinib treatment reduced the co-immunoprecipitation of APP-CTF and gSAP in a concentration-dependent manner. An inactive imatinib derivative (IC200001, see supplementary Fig. 3) served as a negative control. f: In HEK293 cells, APP-CTF without the cytoplasmic domain (APPε-CTF) did not co-immunoprecipitate with gSAP-16K (upper panel); γ-cleavage of APPε-CTF was not stimulated by gSAP-16K in an in vitro assay (lower panel).