Protein topology of presenilin 1

Andrew Doan, Gopal Thinakaran, David R. Borchelt, Hilda H. Slunt, Tamara Ratovitsky, Marcia Podlisny, Dennis J. Selkoe, Mary Seeger, Samuel E. Gandy, Donald L. Price, Sangram S. Sisodia

Research output: Contribution to journalArticlepeer-review

Abstract

Mutations in a gene encoding a multitransmembrane protein, termed presenilin 1 (PS1), are causative in the majority of early-onset cases of AD. To determine the topology of PS1, we utilized two strategies: first, we tested whether putative transmembranes are sufficient to export a protease- sensitive substrate across a lipid bilayer; and second, we examined the binding of antibodies to specific PSi epitopes in cultured cells selectively permeabilized with the pore-forming toxin, streptolysin-O. We document that the 'loop,' N-terminal, and C-terminal domains of PS1 are oriented toward the cytoplasm.

Original languageEnglish (US)
Pages (from-to)1023-1030
Number of pages8
JournalNeuron
Volume17
Issue number5
DOIs
StatePublished - Nov 1996

ASJC Scopus subject areas

  • Neuroscience(all)

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