@entity13017 and XXXX are functionally distinct phosphoproteins.

@entity9761 @entity303 @entity13977 @entity35 @entity13017 @entity5013
UNASSIGNED: Three BRI protein family members have been identified. Among these are @entity9761 and @entity13017 , the latter is associated with Familial Danish and Familial British @entity303 . 'In silico' sequence analysis identified putative @entity13977 binding sites in @entity13017 and @entity9761 . This is singularly important, given that protein phosphorylation is a major mechanism regulating intracellular processes. @entity13977 ( @entity13977 ) interacting proteins (PIPs) are fundamental in determining substrate specificity and subcellular localization of this phosphatase. More than 200 PIPs have thus far been reported. Both @entity13017 and @entity9761 are type II transmembrane glycoproteins relevant in neuronal systems. Using Myc- @entity13017 and Myc- @entity9761 , wild type and @entity13977 binding mutant constructs, it was possible to show, for the first time, that in fact @entity13017 and @entity9761 bind @entity13977 . The complexes @entity13017 : @entity13977 and @entity9761 : @entity13977 were validated in vitro and in vivo. The subcellular distribution of @entity13017 and @entity9761 is similar; both localize to the perinuclear area and Golgi apparatus in non-neuronal cells. However, in SH-SY5Y cells, @entity13017 and @entity9761 could also be detected in elongated cellular projections ('processes') and in @entity35 cortical neurons both are broadly distributed throughout the cell body, @entity5013 and the nucleus. Consistently, co-localization of @entity13017 and @entity9761 with @entity13977 was evident. The functional significance of these complexes is apparent given that both BRI proteins are substrates of @entity13977 , thus simultaneously this is the first report of @entity13017 and @entity9761 as phosphoproteins. Moreover, we show that when @entity13017 is phosphorylated a significant increase in neuronal outgrowth and differentiation is evident. Interestingly, the Alzheimer's amyloid precursor protein (APP), forms a trimeric complex composed of @entity13977 and Fe65, with @entity13977 having the capacity to dephosphorylate APP at Thr668 residue. The emerging consensus appears to be that @entity13977 containing complexes are crucial in regulating signaling events underlying neuropathological conditions.
