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• W2094385558 startingPage "38390" @default.
• W2094385558 abstract "γ-Secretase is composed of the four membrane proteins presenilin, nicastrin, Pen2, and Aph1. These four proteins assemble in a coordinated and regulated manner into a high molecular weight complex. The subunits constitute a total of 19 transmembrane domains (TMD), with many carrying important amino acids involved in catalytic activity, interaction with other subunits, or in ER retention/retrieval of unassembled subunits. We here focus on TMD4 of presenilin 1 (PS1) and show that a number of polar amino acids are critical for γ-secretase assembly and function. An asparagine, a threonine, and an aspartate form a polar interface important for endoplasmic reticulum retention/retrieval. A single asparagine in TMD4 of PS1 is involved in a protein-protein interaction by binding to another asparagine in Pen2. Intriguingly, a charged aspartate in TMD4 is critical for γ-secretase activity, most likely by stabilizing the newly formed complex." @default.
• W2094385558 created "2016-06-24" @default.
• W2094385558 creator A5055769601 @default.
• W2094385558 creator A5059930367 @default.
• W2094385558 creator A5081870658 @default.
• W2094385558 date "2011-11-01" @default.
• W2094385558 modified "2023-09-29" @default.
• W2094385558 title "Polar Transmembrane-based Amino Acids in Presenilin 1 Are Involved in Endoplasmic Reticulum Localization, Pen2 Protein Binding, and γ-Secretase Complex Stabilization" @default.
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• W2094385558 doi "https://doi.org/10.1074/jbc.m111.252429" @default.
• W2094385558 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3207410" @default.
• W2094385558 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21914807" @default.
• W2094385558 hasPublicationYear "2011" @default.
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