Phosphorylation of the cytoplasmic domain of Alzheimer's beta-amyloid precursor protein at Ser655 by a novel protein kinase.

Autor: Isohara T; Laboratory of Molecular and Cellular Neuroscience, Rockefeller University, New York, New York 10021-6399, USA., Horiuchi A, Watanabe T, Ando K, Czernik AJ, Uno I, Greengard P, Nairn AC, Suzuki T
Jazyk: angličtina
Zdroj: Biochemical and biophysical research communications [Biochem Biophys Res Commun] 1999 May 10; Vol. 258 (2), pp. 300-5.
DOI: 10.1006/bbrc.1999.0637
Abstrakt: The cytoplasmic domain of Alzheimer's beta-amyloid precursor protein (APP) can be phosphorylated at Thr654, Ser655, and Thr668 (APP695 isoform numbering). Previous studies demonstrated that Ser655 of APP was phosphorylated by protein kinase C (PKC) and calmodulin-dependent protein kinase II (CaMKII) in vitro and by unidentified protein kinase(s) in vivo. We report here the characterization of a novel protein kinase (designated APP kinase I) which phosphorylates Ser655 of APP. APP kinase I was partially purified over 7,000-fold from rat brain and identified as a approximately 43 kDa protein that is distinct from a number of known protein kinases, including PKC and extracellular signal-regulated kinases (ERKs). The identification of a novel protein kinase that phosphorylates Ser655 will hopefully contribute to our understanding of the metabolism and/or function of APP in the pathogenesis of Alzheimer's disease (AD).
(Copyright 1999 Academic Press.)
Databáze: MEDLINE
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