A single tyrosine residue in the amyloid precursor protein intracellular domain is essential for developmental function

Alessia P.M. Barbagallo, Zilai Wang, Hui Zheng, Luciano D'Adamio

Research output: Contribution to journalArticle

34 Scopus citations

Abstract

The Aβ-precursor protein (APP) intracellular domain is highly conserved and contains many potentially important residues, in particular the 682YENPTY687 motif. To dissect the functions of this sequence in vivo, we created an APP knock-in allele mutating Tyr682 to Gly (Y682G). Crossing this allele to APP-like protein 2 (APLP2) knock-out background showed that mutation of Tyr682 results in postnatal lethality and neuromuscular synapse defects similar to doubly deficient APP/APLP2 mice. Our results demonstrate that a single residue in the APP intracellular region, Tyr682, is indispensable for the essential function of APP in developmental regulation.

Original languageEnglish (US)
Pages (from-to)8717-8721
Number of pages5
JournalJournal of Biological Chemistry
Volume286
Issue number11
DOIs
Publication statusPublished - Mar 18 2011

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ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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