Nuclear signaling: a common function of presenilin substrates?

Abstract	Major progress has recently been made in the characterization of the secretases involved in endoproteolytic processing of the Alzheimer's disease (AD)-associated beta-amyloid precursor protein, betaAPP. betaAPP is the precursor of the amyloid beta-peptide, which is a major constituent of amyloid plaques in the brains of Alzheimer patients. It is now commonly believed that Abeta plays a pivotal role in the pathogenesis of AD, and that inhibiting the production of Abeta may help to treat or to prevent the disease. With beta-secretase and the presenilins, two essential factors in the proteolytic generation of Abeta have now been identified. However, very little is still known about the biological function of the long-known betaAPP. In this review we will discuss a novel putative function of betaAPP in nuclear signaling, an activity, that betaAPP may share with other presenilin substrates such as Notch.
Authors	H Steiner, C Haass
Journal	Journal of molecular neuroscience : MN (J Mol Neurosci) Vol. 17 Issue 2 Pg. 193-8 (Oct 2001) ISSN: 0895-8696 [Print] United States
PMID	11816792 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Review)
Chemical References	APBB1 protein, human Amyloid beta-Protein Precursor Membrane Proteins NOTCH1 protein, human Nerve Tissue Proteins Nuclear Proteins PSEN1 protein, human Presenilin-1 Receptor, Notch1 Receptors, Cell Surface Transcription Factors Acetyltransferases Histone Acetyltransferases KAT5 protein, human Lysine Acetyltransferase 5
Topics	Acetyltransferases (metabolism) Alzheimer Disease (metabolism, physiopathology) Amyloid beta-Protein Precursor (biosynthesis, metabolism) Animals Cell Nucleus (metabolism) Histone Acetyltransferases Humans Lysine Acetyltransferase 5 Membrane Proteins (metabolism) Nerve Tissue Proteins (metabolism) Nuclear Proteins (metabolism) Presenilin-1 Protein Structure, Tertiary (physiology) Receptor, Notch1 Receptors, Cell Surface Signal Transduction (genetics) Transcription Factors

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