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J Biol Chem, Vol. 274, Issue 27, 18851-18856, July 2, 1999
-Amyloid Precursor
Protein Endocytosis, Turnover, and the Generation of Secreted
Fragments, Including A42
,,
,,,
From the It has long been assumed that the C-terminal
motif, NPXY, is the internalization signal for Departments of Psychiatry and Neurobiology & Anatomy, Allegheny University of the Health Sciences, Pittsburgh,
Pennsylvania 15212, the Center for Neurologic Diseases, Harvard
Medical School and Brigham and Women's Hospital, Boston, Massachusetts
02115, and the ¶ Department of Neurosciences, University of
California, San Diego, La Jolla, California 92093
-amyloid
precursor protein (APP) and that the NPXY tyrosine
(Tyr743 by APP751 numbering, Tyr682 in APP695)
is required for APP endocytosis. To evaluate this tenet and to identify
the specific amino acids subserving APP endocytosis, we mutated all
tyrosines in the APP cytoplasmic domain and amino acids within the
sequence GYENPTY (amino acids 737-743). Stable cell lines expressing
these mutations were assessed for APP endocytosis, secretion, and
turnover. Normal APP endocytosis was observed for cells expressing
Y709A, G737A, and Y743A mutations. However, Y738A, N740A, and P741A or
the double mutation of Y738A/P741A significantly impaired APP
internalization to a level similar to that observed for cells lacking
nearly the entire APP cytoplasmic domain (
C), arguing that the
dominant signal for APP endocytosis is the tetrapeptide YENP. Although
not an APP internalization signal, Tyr743 regulates rapid
APP turnover because half-life increased by 50% with the Y743A
mutation alone. Secretion of the APP-derived proteolytic fragment,
A, was tightly correlated with APP internalization, such that A
secretion was unchanged for cells having normal APP endocytosis but
significantly decreased for endocytosis-deficient cell lines.
Remarkably, secretion of the A42 isoform was also reduced in
parallel with endocytosis from internalization-deficient cell lines,
suggesting an important role for APP endocytosis in the secretion of
this highly pathogenic A species.
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