Intramembrane Proteolysis in Regulated Protein Trafficking
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چکیده
منابع مشابه
Nuclear localization of amyloid-β precursor protein-binding protein Fe65 is dependent on regulated intramembrane proteolysis
Fe65 is an adaptor protein involved in both processing and signaling of the Alzheimer-associated amyloid-β precursor protein, APP. Here, the subcellular localization was further investigated using TAP-tagged Fe65 constructs expressed in human neuroblastoma cells. Our results indicate that PTB2 rather than the WW domain is important for the nuclear localization of Fe65. Electrophoretic mobility ...
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Regulated intramembrane proteolysis (Rip) is an ancient and widespread process by which cells transmit information from one compartment (the endoplasmic reticulum) to another (the nucleus). Two separate cleavages that are carried out by two separate proteases are required for Rip. The first protease cleaves its protein substrate within an extracytoplasmic domain; the second cleaves it within a ...
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Intramembrane cleavage of transmembrane proteins is a fundamental cellular process. Several enzymes capable of releasing domains of integral membrane proteins have been described. Transmembrane protein proteolytic cleavage is regulated and involved not only in degrading membrane spanning segments but also in generating messengers that elicit biological responses. This review examines the role o...
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Regulated Intramembrane Proteolysis (RIP) is a highly conserved signaling mechanism, where a signaling molecule is cleaved within the lipid bilayer by an intramembrane protease. Traditional wisdom argued that proteolysis requires water; however, in RIP, both the protease and the substrate are integral membrane proteins and the cleavage occurs within the hydrophobic lipid bilayer. It has been mo...
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ژورنال
عنوان ژورنال: Traffic
سال: 2011
ISSN: 1398-9219
DOI: 10.1111/j.1600-0854.2011.01219.x