Title : Phosphorylation of a tyrosine in the amyloid-beta protein precursor intracellular domain inhibits Fe65 binding and signaling.

Pub. Date : 2009

PMID : 19221419






5 Functional Relationships(s)
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Protein Name
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1 Phosphorylation of a tyrosine in the amyloid-beta protein precursor intracellular domain inhibits Fe65 binding and signaling. Tyrosine amyloid beta precursor protein binding family B member 1 Homo sapiens
2 Here we report that phosphorylation of Tyr-682 inhibits the interactions between AbetaPP and Fe65, which is the main regulatory mechanism controlling Fe65 nuclear signaling. Tyrosine amyloid beta precursor protein binding family B member 1 Homo sapiens
3 Here we report that phosphorylation of Tyr-682 inhibits the interactions between AbetaPP and Fe65, which is the main regulatory mechanism controlling Fe65 nuclear signaling. Tyrosine amyloid beta precursor protein binding family B member 1 Homo sapiens
4 Furthermore, we show that tyrosine phosphorylation of AbetaPP also inhibits interaction of the two other Fe65 family members, Fe65L1 and Fe65L2. Tyrosine amyloid beta precursor protein binding family B member 1 Homo sapiens
5 Our results indicate that phosphorylation of the cytoplasmic tail of AbetaPP on Tyr-682 represents a second mechanism, alternative to AbetaPP processing by secretases, that regulates AbetaPP/Fe65 downstream signaling pathways. Tyrosine amyloid beta precursor protein binding family B member 1 Homo sapiens