Table 1.
APP source | G-protein | Citation |
---|---|---|
APP695 wt; peptide 20 (H657-L676 | Gαo∗; not Gαs, Gαi1, 2, 3, | Nishimoto et al., 1993 |
Peptide 20 (H657-L676) | Gαo/i; not Gαs | Colombo et al., 1994; Lang et al., 1995 |
APP695 wt | Gαo∗; not Gαi2 | Okamoto et al., 1995 |
APP695 wt | Gαo∗ | Okamoto et al., 1996 |
APP695 wt, V642I, V642F, V642G | Gαo∗#; not Gαs, Gαi2, Gαz | Ikezu et al., 1996 |
APP695 V642I, V642F, V642G | Gαo#; not Gαi2 | Yamatsuji et al., 1996a |
APP695 V642I, V642F, V642G | Gαo; not Gαi2 | Yamatsuji et al., 1996b |
APP695 V642I | Gαo#; not Gαt | Giambarella et al., 1997 |
APP695 wt | Gαo∗#; not Gαi2 or Gαs# | Brouillet et al., 1999 |
APP695 V642I | Gαo/i† | Hashimoto et al., 2000 |
APP695 wt, V642I | Gαo/i† | Sudo et al., 2000 |
APP695 wt, V642I | Gαo/i† | Niikura et al., 2000 |
APP695 wt | Gαo/i† | Mbebi et al., 2002 |
APP695 wt | Gαo; not Gαi1 | Hashimoto et al., 2003a |
EGFR-APPicd chimera | Gαo/i† | Hashimoto et al., 2003b |
APP695 V642I, APP695 KM595-6NL | Gαo | McPhie et al., 2003 |
APP695 wt, V642I | Gαo/i† | Niikura et al., 2004 |
APP695 wt | Gαo/i | Xu et al., 2009 |
APP695 wt | Gαo; not Gαi2, Gαi3, | Sola Vigo et al., 2009 |
APP695 wt | Gαo† | Shaked et al., 2009 |
APPL (Manduca, Drosophila) | Gαo∗; not Gαi, Gαs | Ramaker et al., 2013 |
APP695 wt | Gαo∗; not Gαs | Ramaker et al., 2013 |
APP695 wt | Gαo∗ | Fogel et al., 2014 |
APP695 wt | Gαo/i† | Milosch et al., 2014 |
APPL (Manduca) | Gαo | Ramaker et al., 2016a |
Membrane-tethered AICD | Gαs∗∗ | Deyts et al., 2012 |
Summary of published evidence that APP interacts with Gαo (but usually not other G proteins, including Gαs, Gαz, and Gαi isofroms). The table includes studies on both wild type APP695, isolated peptide 20 constructs (containing the G protein-binding domain of APP695), and FAD-associated mutant forms of APP with altered residues at V642 (indicated in the left-hand column). Studies that showed direct binding between Gαo and APP/APPL are indicated with an asterisk (∗). Studies that used PTX to indicate the involvement of Gαo/i family proteins are indicated with a cross (\dagger). Studies that used CTX to indicate the absence of Gαs-dependent signaling is indicated with a hash mark (#). Study that showed direct binding between Gαs and constructs containing the G protein-binding domain is indicated with a double asterisk (∗∗). Citations for each set of results are shown in the right-hand column. ∗Studies that showed direct binding between Gαo and APP/APPL (or the G protein-binding domain). †Studies that demonstrated sensitivity to PTX, indicating the involvement of Gαo/i. #Studies that tested sensitivity to CTX, indicating the absence of Gαs-dependent signaling. ∗∗Study that showed direct binding between Gαs and peptides containing the G protein-binding domain.