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. 2007 Jan 17;27(3):574–581. doi: 10.1523/JNEUROSCI.5094-06.2007

Figure 1.

Figure 1.

In vivo phosphorylation of PAR-1 at T408 and its importance in regulating PAR-1 activity. A–D, Scanning electron microscopic images of transgenic fly eyes overexpressing wild-type (WT) PAR-1 (A), PAR-1(T408A) (B), PAR-1(T408E) (C), or wild-type control (D) fly eyes. E, F, Western blot analysis showing that whereas PAR-1 overexpression caused an approximate fourfold increase in wild-type h-tau (E) or h-tau(R406W) (F) phosphorylation at 12E8 sites, PAR-1(T408A) or PAR-1(T408E) had little effects. Tubulin served as a loading control. G, Detection of T408 phosphorylation of wild-type PAR-1 but not PAR-1(T408A) or PAR-1(T408E) produced from transgenes (bottom). Exogenous PAR-1 proteins expressed from the transgenes were tagged with a myc tag and detected with an anti-myc antibody. H, Detection of p-T408-positive endogenous PAR-1 protein from adult fly head extracts prepared from wild-type and hypomorphic PAR-1 (PAR-1W3/PAR-119A) mutant animals. ←, PAR-1-specific bands; *, nonspecific bands.