Dataset

DZNE-2025-00816

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Dataset: Identification of naturally short gamma-secretase substrates

Müller, S. A.DZNE* ; Lichtenthaler, S.DZNE*

2024
PRoteomics IDEntifications Database

Abstract: The intramembrane protease gamma-secretase has broad physiological functions, but also contributes to Notch-dependent tumors and Alzheimer’s disease. To identify naturally short substrates and non-substrates of gamma-secretase, we used four human cell lines of different tissue origins, breast cancer MCF7 cells, cervix carcinoma HeLa cells, T cell leukemia Jurkat cells and lymphoma U937 macrophage-like cells. The cell lines were treated overnight with the established gamma-secretase inhibitor DAPT or DMSO as a control. The proteomes of membrane fractions were determined by nano-liquid chromatography-tandem mass spectrometry and label-free quantitative proteomics. TNFRSF12A, PTPRCAP and C16orf54 were identified as potential naturally short gamma-secretase substrates, whereas other proteins with a short ectodomain including ‘pituitary tumor-transforming gene 1-interacting protein’ (PTTG1IP) did not show an increased abundance upon DAPT treatment.

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Contributing Institute(s):

1. Neuroproteomics (AG Lichtenthaler)

Research Program(s):

1. 352 - Disease Mechanisms (POF4-352) (POF4-352)

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Linked articles:

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Journal Article Aßfalg, M. (First author)DZNE* ; Güner, G.DZNE* ; Müller, S. A.DZNE* ; Breimann, S.DZNE* ; Langosch, D. ; Muhle-Goll, C. ; Frishman, D. ; Steiner, H.DZNE* ; Lichtenthaler, S. F. (Last author)DZNE*
Cleavage efficiency of the intramembrane protease γ-secretase is reduced by the palmitoylation of a substrate's transmembrane domain.
The FASEB journal 38(2), e23442 (2024) [10.1096/fj.202302152R]2024   Files BibTeX | EndNote: XML, Text | RIS

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