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. 2010 Apr 28;285(27):20664–20674. doi: 10.1074/jbc.M109.055608

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© 2010 by The American Society for Biochemistry and Molecular Biology, Inc.

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FIGURE 7. — TMEM59 inhibits glycosylation of different proteins. HEK293 cells were transiently transfected with the indicated constructs and either control vector (con) or TMEM59. GFP served as transfection control, where indicated. Lysates (lys) and supernatants (sup) were blotted against TMEM59 (93) and the indicated proteins. A, lysates of BACE1 transfected cells were treated with N-glycosidase F (+F) or endoglycosidase H (+H), controls remained untreated (−F, −H). The samples were blotted against BACE1 (EE-17, ***, mature, **, immature, and *, de-glycosylated BACE1) and TMEM59 (93). As a control, APP was deglycosylated in the same manner, revealing that TMEM59 does not affect the core N-glycosylation, but only the complex glycosylation (mature form) of APP. B, transfected PrP was detected in the lysate (3F4, **, complex glycosylated and *, di-/mono-/unglycosylated forms of PrP). C, secreted alkaline phosphatase (HA-SEAP) was detected in the supernatant (after immunoprecipitation) or in lysate (**, mature and *, immature SEAP) and detected with anti-HA antibody. D, transfected APPsβ was detected in the supernantant (192wt) and TMEM59 in the lysate (93). E, FLAG-TNFα-HA was transfected. fl-TNFα and TNFα-NTF were detected in the lysate (FLAG), secreted TNFα (HA) in the supernatant.