PubMed Journals: Biochemistry
Source: PMID: 9109675
⇦ ⇨ Biochemistry. 1997 Apr 15;36(15):4643-9.
Phosphorylation of Alzheimer beta-amyloid
Suzuki T(1), Ando K, Isohara T, Oishi M,
Lim GS, Satoh Y, Wasco W, Tanzi RE, Nairn
AC, Greengard P, Gandy SE, Kirino Y.
(1) Graduate School of Pharmaceutical Sciences,
University of Tokyo, Japan.
Amyloid precursor-like proteins (APLPs),
APLP1 and APLP2, are members of a gene family
which include the Alzheimer beta-amyloid
precursor protein (APP). APLP1, APLP2, and
APP contain highly homologous amino acid
sequences, especially in their cytoplasmic
domains, although APLPs lack the beta-amyloid
domain derived by proteolytic processing
from APP. APP is phosphorylated at three
sites in the cytoplasmic domain in cultured
cells and adult rat brain [Suzuki et al.
(1994) EMBO J. 13, 1114-1122; Oishi, et al.
(1997) Mol. Med. 3, 109-121] and at sites
in the extracellular domain in cultured
cells [Knops et al. (1993) Biochem. Biophys.
Res. Commun. 197, 380-385; Hung & Selkoe
(1994) EMBO J. 13, 534-542; Walter et al.
(1997) J. Biol. Chem. 272, 1896-1903]. We
report here that a cytoplasmic domain peptide
from APLP1 is phosphorylated in vitro by
protein kinase C and that a cytoplasmic
domain peptide from APLP2 is phosphorylated
in vitro by protein kinase C and cdc2 kinase.
APLP2 is phosphorylated by cdc2 kinase at
a site homologous to the cdc2 kinase site
phosphorylated in APP. Furthermore, phosphorylation
of this site occurs in a cell cycle-dependent
manner in cultured cells. These findings
indicate that in intact cells the phosphorylation
of APLP2 appears to be regulated in a similar
fashion to that of APP.
DOI: 10.1021/bi962618k PMID: 9109675 [Indexed