Journal
MOLECULAR AND CELLULAR NEUROSCIENCE
Volume 20, Issue 1, Pages 13-20Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1006/mcne.2002.1108
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Funding
- MRC [G0000749] Funding Source: UKRI
- Medical Research Council [G0000749] Funding Source: Medline
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Mutations in the Presenilin 1 gene are the cause of the majority of autosomal dominant familial forms of Alzheimer's disease. Presenilin 1 (PS1) is produced as a holoprotein but is then rapidly processed to amino- (N-PS1) and carboxy-terminal (C-PS1) fragments that are incorporated into stable high molecular mass complexes. The mechanisms that control PS1 cleavage and stability are not property understood but sequences within C-PS1 have been shown to regulate both of these properties. Here we demonstrate that cyclin dependent kinase-5/p35 (cdk5/p35) phosphorylates PS1 on threonine(354) within CPS1 both in vitro and in vivo. Threonine(354) phosphorylation functions to selectively stabilize G-PS1. Our results demonstrate that cdk5/p35 is a regulator of PS1 metabolism.
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