Description
APPL1, an adaptor protein containing an NH2-terminalBin/Amphiphiphysin/Rvs (BAR) domain, a central pleckstrin homology (PH) domain and a COOH-terminal phosphotyrosine binding (PTB) domain [1], was originally identified as an interacting partner of Akt in a yeast two-hybrid assay using Akt2 as a bait [2]. APPL1 binds to a number of cell surface receptors (TrkA[3, 4], DCC[5], adiponectin [6, 7], FSH[8]) and intracellular signaling molecules (small GTPase Rab5[9], GIPC[4] and inositol 5-phosphatase[10], suggesting that APPL1 may act as a common relay to coordinate diverse signaling cascades. APPL1 potentiates insulin-mediated Akt activation by counteracting the effect of the Akt inhibitor TRB3 [11].
Total 739AA, Mw: 83.2 kDa (calculated). N-terminal His-tag and TEV cleavage site, 31 extra AA