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- W3154792201 abstract "Receptor tyrosine kinase (RTK)-mediated activation of downstream effector pathways such as the RAS GTPase/MAP kinase (MAPK) signaling cascade is thought to occur exclusively from lipid membrane compartments in mammalian cells. Here, we uncover a membraneless, protein granule-based subcellular structure that can organize RTK/RAS/MAPK signaling in cancer. Chimeric (fusion) oncoproteins involving certain RTKs including ALK and RET undergo de novo higher-order assembly into membraneless cytoplasmic protein granules. These pathogenic biomolecular condensates locally concentrate the RAS activating complex GRB2/SOS1 and activate RAS in a lipid membrane-independent manner to initiate MAPK signaling. Formation of membraneless protein granules by RTK oncoproteins is both necessary and sufficient for RAS/MAPK signaling output in cells. Our findings reveal membraneless, higher-order cytoplasmic protein assembly as a distinct subcellular platform to activate RTKs and RAS GTPases and a general principle by which cells can organize oncogenic signaling." @default.
- W3154792201 created "2021-04-26" @default.
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- W3154792201 date "2020-01-01" @default.
- W3154792201 modified "2023-10-14" @default.
- W3154792201 title "Kinase-Mediated RAS Signaling Via Membraneless Cytoplasmic Protein Granules" @default.
- W3154792201 doi "https://doi.org/10.2139/ssrn.3578156" @default.
- W3154792201 hasPublicationYear "2020" @default.
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