Cited by 189Protein Kinase Regulation and GTPase SignalingRNA Research and SplicingCellular transport and secretion

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Kinase-mediated RAS signaling via membraneless cytoplasmic protein granules

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Tulpule, Asmin, Guan, Juan, Neel, Dana S., Allegakoen, Hannah R., Lin, Yone Phar, Brown, David, Chou, Yu-Ting, Heslin, Ann, Chatterjee, Nilanjana, Perati, Shriya, Menon, Shruti, Nguyen, Tan A., Debnath, Jayanta, Ramirez, Alejandro D., Shi, Xiaoyu, Yang, Bin, Feng, Siyu, Makhija, Suraj, Huang, Bo, Bivona, Trever G.·2021·Cell

DOI 10.1016/j.cell.2021.03.031PMC PMC8127962

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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 that actively signal. These pathogenic biomolecular condensates locally concentrate the RAS activating complex GRB2/SOS1 and activate RAS in a lipid membrane-independent manner. RTK protein granule formation is critical for oncogenic RAS/MAPK signaling output in these cells. We identify a set of protein granule components and establish structural rules that define the formation of membraneless protein granules by RTK oncoproteins. Our findings reveal membraneless, higher-order cytoplasmic protein assembly as a distinct subcellular platform for organizing oncogenic RTK and RAS signaling.

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Authors: Tulpule, A., Guan, J., Neel, D. S., Allegakoen, H. R., Lin, Y. P., Brown, D., Chou, Y.-T., Heslin, A., Chatterjee, N., Perati, S., Menon, S., Nguyen, T. A., Debnath, J., Ramirez, A. D., Shi, X., Yang, B., Feng, S., Makhija, S., Huang, B., & Bivona, T. G.
Affiliations: University of California, San Francisco (US)
Corresponding author: Huang, Bo
Bivona, Trever G.
ORCID: Tulpule, Asmin
Guan, Juan
Neel, Dana S.
Allegakoen, Hannah R.
Lin, Yone Phar
Chou, Yu-Ting
Chatterjee, Nilanjana
Perati, Shriya
Menon, Shruti
Nguyen, Tan A.
Debnath, Jayanta
Shi, Xiaoyu
Yang, Bin
Feng, Siyu
Makhija, Suraj
Huang, Bo
Bivona, Trever G.
Venue: Cell
Publisher: Elsevier BV
Published: 2021-05
Volume: 184
Issue: 10
Pages: 2649-2664.e18
ISSN: 0092-8674 (ISSN-L)
DOI: 10.1016/j.cell.2021.03.031
PMC: PMC8127962
OpenAlex: W3155633297
Cited by: 189
References: 67
Citations by year: 2026: 25 · 2025: 35 · 2024: 36 · 2023: 46 · 2022: 27 · 2021: 18
FWCI: 7.54
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
creativecommons.org/licenses/by/4.0/ (vor)
Locations: Cell (publishedVersion, cc-by)
SSRN Electronic Journal (publishedVersion)
bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: NIH
NCI Cancer Moonshot
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Keywords: biomolecular condensates, receptor tyrosine kinase, RAS/MAPK pathway, anaplastic lymphoma kinase, RET, fusion oncoproteins, cancer signaling
MeSH terms: Biomolecular Condensates, Cytoplasmic Granules, Enzyme Activation, Humans, Neoplasms, Signal Transduction, Oncogene Proteins, Fusion, ras Proteins, SOS1 Protein, Adaptor Proteins, Signal Transducing, GRB2 Adaptor Protein, HEK293 Cells

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