NDLI: ADAM10, the rate-limiting protease of regulated intramembrane proteolysis of Notch and other proteins, is processed by ADAMS-9, ADAMS-15, and the gamma-secretase.

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ADAM10, the rate-limiting protease of regulated intramembrane proteolysis of Notch and other proteins, is processed by ADAMS-9, ADAMS-15, and the gamma-secretase.

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ADAM10, the rate-limiting protease of regulated intramembrane proteolysis of Notch and other proteins, is processed by ADAMS-9, ADAMS-15, and the gamma-secretase.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Jorissen, Ellen De Strooper, Bart Tousseyn, Thomas Konietzko, Uwe Annaert, Wim Snellinx, An Hartmann, Dieter Thathiah, Amantha Serneels, Lutgarde Reiss, Karina Nyabi, Omar Raemaekers, Tim Maes, Elke Saftig, Paul
Description	Author Affiliation: Tousseyn T ( Center for Human Genetics, Katholieke Universiteit Leuven (K. U. Leuven), Department for Developmental and Molecular Genetics, and Laboratory of Membrane Trafficking, Vlaams Instituut voor Biotechnologie (VIB), K. U. Leuven, B-3000 Leuven, Belgium.)
Abstract	ADAM10 is involved in the proteolytic processing and shedding of proteins such as the amyloid precursor protein (APP), cadherins, and the Notch receptors, thereby initiating the regulated intramembrane proteolysis (RIP) of these proteins. Here, we demonstrate that the sheddase ADAM10 is also subject to RIP. We identify ADAM9 and -15 as the proteases responsible for releasing the ADAM10 ectodomain, and Presenilin/gamma-Secretase as the protease responsible for the release of the ADAM10 intracellular domain (ICD). This domain then translocates to the nucleus and localizes to nuclear speckles, thought to be involved in gene regulation. Thus, ADAM10 performs a dual role in cells, as a metalloprotease when it is membrane-bound, and as a potential signaling protein once cleaved by ADAM9/15 and the gamma-Secretase.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	17
Volume Number	284
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2009-04-24
Publisher Place	United States
Access Restriction	Open
Subject Keyword	ADAM Proteins Metabolism Physiology Amyloid Precursor Protein Secretases Gene Expression Regulation, Enzymologic Membrane Proteins Receptors, Notch Animals Cell Nucleus Mice Microscopy, Fluorescence Presenilins Protein Structure, Tertiary Signal Transduction Subcellular Fractions Tissue Distribution Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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