Journal
LIFE SCIENCE ALLIANCE
Volume 5, Issue 6, Pages -Publisher
LIFE SCIENCE ALLIANCE LLC
DOI: 10.26508/lsa.202201380
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Funding
- Swiss National Science Foundation [SNF_31003A_165860/1, SNF_310030_188793]
- Childhood Cancer Foundation
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This study using spatial proteomics approach found that hepatocyte growth factor (HGF) can change the composition of the plasma membrane-associated proteome of Medulloblastoma (MB) tumor cells, thereby affecting cell adhesion and invasiveness. The study also revealed the important role of MAP4K4 in controlling the plasma membrane-associated proteome of MB cells.
The composition of the plasma membrane (PM)-associated proteome of tumor cells determines cell-cell and cell-matrix interactions and the response to environmental cues. Whether the PM-associated proteome impacts the phenotype of Medulloblastoma (MB) tumor cells and how it adapts in response to growth factor cues is poorly understood. Using a spatial proteomics approach, we observed that hepatocyte growth factor (HGF)-induced activation of the receptor tyrosine kinase c-MET in MB cells changes the abundance of transmembrane and membrane-associated proteins. The depletion of MAP4K4, a pro-migratory effector kinase downstream of c-MET, leads to a specific decrease of the adhesion and immunomodulatory receptor CD155 and of components of the fast-endophilin- mediated endocytosis (FEME) machinery in the PM-associated proteome of HGF-activated MB cells. The decreased surface expression of CD155 or of the fast-endophilin-mediated endocytosis effector endophilin-A1 reduces growth and invasiveness of MB tumor cells in the tissue context. These data thus describe a novel function of MAP4K4 in the control of the PM-associated proteome of tumor cells and identified two downstream effector mechanisms controlling proliferation and invasiveness of MB cells.
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