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• W1965562743 startingPage "1068" @default.
• W1965562743 abstract "APH-1 is one of the four essential components of the presenilin-γ-secretase complex and has two human homologs, APH-1a, and APH-1b, both of which are seven-pass membrane proteins. Here, we identified a novel splice variant of human APH-1b. This variant lacks exon 4, which encodes the entire fourth transmembrane domain. The mRNA expression of this variant was detected in most tissues at low levels. In transiently transfected cells, protein expression of the APH-1b variant was much lower than that of the wild-type. Furthermore, exogenous expression of the APH-1-interacting protein, nicastrin, significantly increased the variant protein levels. These data suggest that the APH-1b variant protein is destabilized, and implies that the fourth transmembrane domain plays an important role in the protein stability and function of APH-1." @default.
• W1965562743 created "2016-06-24" @default.
• W1965562743 creator A5039068085 @default.
• W1965562743 creator A5057535269 @default.
• W1965562743 creator A5059736273 @default.
• W1965562743 date "2005-05-01" @default.
• W1965562743 modified "2023-09-27" @default.
• W1965562743 title "Identification and characterization of a novel human APH-1b splice variant lacking exon 4" @default.
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• W1965562743 doi "https://doi.org/10.1016/j.bbrc.2005.03.096" @default.
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