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Saccharomyces cerevisiae Models of Alzheimer's Disease to Screen Genes, Mutations, and Chemicals Affecting Amyloid Beta Production by γ-Secretase

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MUC1 is a substrate for gamma-secretase.

Joanne Julian¹, Neeraja Dharmaraj, Daniel D Carson

¹Department of Biological Sciences, University of Delaware, Newark, Delaware 19716, USA.

Journal of Cellular Biochemistry

|August 28, 2009

Summary

This study reveals how normal cells process the MUC1 protein's cytoplasmic tail via TACE/ADAM17 and gamma-secretase, preventing oncogenic signaling. This pathway, involving MUC1-CTF15 fragment accumulation, is conserved in normal and tumor cells.

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Recording Gamma Band Oscillations in Pedunculopontine Nucleus Neurons

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Published on: September 14, 2016

Area of Science:

Cell Biology
Molecular Biology
Cancer Biology

Background:

MUC1 signaling in normal and cancer cells requires understanding MUC1 cytoplasmic tail processing.
The oncogenic potential of MUC1 necessitates defining its processing pathways.

Purpose of the Study:

To elucidate the MUC1 cytoplasmic tail processing pathway initiated by TACE/ADAM17 cleavage.
To investigate the role of presenilin-dependent gamma-secretase in MUC1 processing.
To determine if this pathway is conserved in normal and tumor-derived cells.

Main Methods:

Utilized human uterine epithelial cell line (HES) and tumor-derived cells.
Employed gamma-secretase inhibitors and TACE/ADAM17 inhibitors.
Used nicastrin siRNA to reduce gamma-secretase complex activity.
Performed co-immunoprecipitation to detect protein complexes.

Main Results:

Endogenous MUC1 undergoes regulated intramembranous proteolysis mediated by gamma-secretase.
Gamma-secretase inhibition led to accumulation of MUC1 C-terminal fragment (CTF15).
TACE/ADAM17 inhibition reduced CTF15 accumulation and MUC1 ectodomain release.
Nicastrin siRNA also caused CTF15 accumulation, and CTF15 co-immunoprecipitated with nicastrin.
The MUC1 processing pathway is conserved across normal and tumor cells from humans and mice.

Conclusions:

MUC1 processing involves TACE/ADAM17 cleavage followed by gamma-secretase-mediated intramembranous proteolysis.
This pathway efficiently attenuates potential signaling from MUC1 cytoplasmic tail fragments.
The conserved nature of this pathway suggests a fundamental mechanism for regulating MUC1's role in normal physiology and cancer.