PubMed Journals: Biochemistry

  Source:		PMID: 9109675

    		Biochemistry. 1997 Apr 15;36(15):4643-9.
			Phosphorylation of Alzheimer beta-amyloid
			precursor-like proteins.

			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.

			Author Information
			(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
			for MEDLINE]

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