A nine-transmembrane domain topology for presenilin 1 (Q28263814)

7

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Bengt Winblad

6

object named as

Bengt Winblad

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author name string

Hanna Laudon

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Emil M Hansson

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Karin Melén

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Anna Bergman

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Mark R Farmery

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Jan Näslund

Journal of Biological Chemistry

9

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language of work or name

English

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publication date

21 October 2005

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published in

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volume

280

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issue

42

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page(s)

35352-60

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cites work

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Photoactivated gamma-secretase inhibitors directed to the active site covalently label presenilin 1

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Aph-1, Pen-2, and Nicastrin with Presenilin generate an active gamma-Secretase complex

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Gamma-secretase exists on the plasma membrane as an intact complex that accepts substrates and effects intramembrane cleavage

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The extreme C terminus of presenilin 1 is essential for gamma-secretase complex assembly and activity

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The presenilin C-terminus is required for ER-retention, nicastrin-binding and gamma-secretase activity

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Detergent-dependent dissociation of active gamma-secretase reveals an interaction between Pen-2 and PS1-NTF and offers a model for subunit organization within the complex

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Identification of a novel PSD-95/Dlg/ZO-1 (PDZ)-like protein interacting with the C terminus of presenilin-1

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X11 alpha and x11 beta interact with presenilin-1 via their PDZ domains

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Interaction with telencephalin and the amyloid precursor protein predicts a ring structure for presenilins

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A signal peptide peptidase (SPP) reporter activity assay based on the cleavage of type II membrane protein substrates provides further evidence for an inverted orientation of the SPP active site relative to presenilin

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Consensus analysis of signal peptide peptidase and homologous human aspartic proteases reveals opposite topology of catalytic domains compared with presenilins

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Presenilin Proteins Undergo Heterogeneous Endoproteolysis between Thr291and Ala299and Occur as Stable N- and C-Terminal Fragments in Normal and Alzheimer Brain Tissue

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