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• W2056541782 startingPage "782" @default.
• W2056541782 abstract "Stimulation of macrophages with phorbolesters, bacterial DNA, or lipopolysaccharides causes regulated intramembrane proteolysis or RIPping of the CSF-1 receptor. This process involves TACE-mediated cleavage in the extracellular domain, followed by γ-secretase-mediated cleavage within the transmembrane region. In the current study, we have identified the TACE cleavage site, which is present twelve residues from the carboxy-terminal end of the extracellular domain. Replacement of fourteen residues at the end of the extracellular domain blocked TACE cleavage. In addition, we identified the γ-secretase cleavage site, which is present four residues from the carboxy-terminal end of the transmembrane region. Replacement of six residues surrounding this site strongly reduced intramembrane cleavage. Our results provide new insights into the molecular physiology of the CSF-1 receptor and contribute to our understanding of substrate selection by TACE and γ-secretase." @default.
• W2056541782 created "2016-06-24" @default.
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• W2056541782 creator A5071465039 @default.
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• W2056541782 date "2014-07-01" @default.
• W2056541782 modified "2023-09-27" @default.
• W2056541782 title "Identification and mutagenesis of the TACE and γ-secretase cleavage sites in the colony-stimulating factor 1 receptor" @default.
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• W2056541782 doi "https://doi.org/10.1016/j.bbrc.2014.06.061" @default.
• W2056541782 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24955855" @default.
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