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A USP28-TM9SF3-Golgiphagy axis maintains glycosylation homeostasis and promotes breast cancer progression.
EMBO Journal · · Journal Article
Xu, Cai + more
Abstract ↗AI summary
The abstract is read at the publisher; the summary is JClub's.
USP28 regulates Golgiphagy by stabilizing TM9SF3, and its inhibition suppresses breast cancer growth in models.
- Why it matters: Understanding Golgiphagy's regulation is crucial because it maintains Golgi function and glycosylation fidelity, which are linked to cancer progression.
- What they did: The study used proteomic and functional analyses to show that USP28 removes ubiquitin from TM9SF3, promoting Golgiphagy and glycosylation homeostasis, with effects on breast cancer cell proliferation.
- The result: Inhibiting USP28 or TM9SF3 reduces Golgiphagy, disrupts glycosylation, and markedly suppresses tumor growth, highlighting this pathway as a potential therapeutic target.
The findingWhy it mattersWhat they didThe result