Proteomics

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Identification of naturally short gamma-secretase substrates

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.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Stephan Mueller  

LAB HEAD: Stefan F. Lichtenthaler

PROVIDER: PXD045701 | Pride | 2024-05-24

REPOSITORIES: Pride

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Hela_Gamma_DAPT_1.raw Raw
Hela_Gamma_DAPT_2.raw Raw
Hela_Gamma_DAPT_4.raw Raw
Hela_Gamma_DAPT_5.raw Raw
Hela_Gamma_DMSO_1.raw Raw
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Publications

Cleavage efficiency of the intramembrane protease γ-secretase is reduced by the palmitoylation of a substrate's transmembrane domain.

Aßfalg Marlene M   Güner Gökhan G   Müller Stephan A SA   Breimann Stephan S   Langosch Dieter D   Muhle-Goll Claudia C   Frishman Dmitrij D   Steiner Harald H   Lichtenthaler Stefan F SF  

FASEB journal : official publication of the Federation of American Societies for Experimental Biology 20240201 2

The intramembrane protease γ-secretase has broad physiological functions, but also contributes to Notch-dependent tumors and Alzheimer's disease. While γ-secretase cleaves numerous membrane proteins, only few nonsubstrates are known. Thus, a fundamental open question is how γ-secretase distinguishes substrates from nonsubstrates and whether sequence-based features or post-translational modifications of membrane proteins contribute to substrate recognition. Using mass spectrometry-based proteomic  ...[more]

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