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aph-1 and pen-2 are required for Notch pathway signaling, gamma-secretase cleavage of betaAPP, and presenilin protein accumulation.

Abstract：

:Presenilins are components of the gamma-secretase protein complex that mediates intramembranous cleavage of betaAPP and Notch proteins. A C. elegans genetic screen revealed two genes, aph-1 and pen-2, encoding multipass transmembrane proteins, that interact strongly with sel-12/presenilin and aph-2/nicastrin. Human aph-1 and pen-2 partially rescue the C. elegans mutant phenotypes, demonstrating conserved functions. The human genes must be provided together to rescue the mutant phenotypes, and the inclusion of presenilin-1 improves rescue, suggesting that they interact closely with each other and with presenilin. RNAi-mediated inactivation of aph-1, pen-2, or nicastrin in cultured Drosophila cells reduces gamma-secretase cleavage of betaAPP and Notch substrates and reduces the levels of processed presenilin. aph-1 and pen-2, like nicastrin, are required for the activity and accumulation of gamma-secretase.

journal_name

Dev Cell

journal_title

Developmental cell

authors

Francis R,McGrath G,Zhang J,Ruddy DA,Sym M,Apfeld J,Nicoll M,Maxwell M,Hai B,Ellis MC,Parks AL,Xu W,Li J,Gurney M,Myers RL,Himes CS,Hiebsch R,Ruble C,Nye JS,Curtis D

doi

10.1016/s1534-5807(02)00189-2

keywords:

subject

Has Abstract

pub_date

2002-07-01 00:00:00

pages

85-97

issue

1

eissn

1534-5807

issn

1878-1551

pii

S1534-5807(02)00189-2

journal_volume

3

pub_type

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