The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Ras/MAPK signaling from endomembranes
Abstract
Signal transduction along the Ras/MAPK pathway has been generally thought to take place at the plasma membrane. It is now evident that the plasma membrane is not the only platform capable of Ras/MAPK signal induction. Fusion of Ras with green fluorescent protein and the development of genetically encoded fluorescent probes for Ras activation have revealed signaling events on a variety of intracellular membranes including endosomes, the Golgi apparatus and the endoplasmic reticulum. Thus, the Ras/MAPK pathway is spatially compartmentalized within cells and this may afford greater complexity of signal output.
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In cultured cells, Dab2 modulates endosomal Ras/MAPK (Erk1/2) activity by regulating the disassembly of Grb2/Sos1 complexes associated with clathrin-coated vesicles.
“In cultured cells, Dab2 modulates endosomal Ras/MAPK (Erk1/2) activity by regulating the disassembly of Grb2/Sos1 complexes associated with clathrin-coated vesicles”
From Endocytosis and Physiology: Insights from Disabled-2 Deficient Mice (2016) · cites this paper as Fehrenbacher et al., 2009
The “Ras Signalling on endosomes” section (page unavailable) describes endosomal Ras/MAPK signaling and reports Grb2 and mSOS on endosomes. The copy does not mention Dab2 or say that it regulates disassembly of Grb2/Sos1 complexes on clathrin-coated vesicles; searches for Dab2 and the proposed mechanism found no such passage. (LLM, conf=0.83)
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Ras signalling on the endoplasmic reticulum and the Golgi
Chiu, V. K., Bivona, T., Hach, A., Sajous, J. B., Silletti, J., Wiener, H., Johnson, R. L., Cox, A. D., & Philips, M. R. (2002) · Nature Cell Biology · doi:10.1038/ncb783 · Cited by 594 · cited 17×
“These observations raise the obvious question of whether endomembrane associated Ras is capable of signaling and, perhaps more important, whether the signal output varies depending on the subcellular platform? Fluorescent probes of Ras activity have been used to address this question and the answer appears to be, yes;…”
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Tsang, M., Friesel, R., Kudoh, T., & Dawid, I. B. (2002) · Nature Cell Biology · doi:10.1038/ncb749 · Cited by 304
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Cited by
Sorted by citations
Ras Conformational Ensembles, Allostery, and Signaling
Lu, S., Jang, H., Muratcioglu, S., Gursoy, A., Keskin, O., Nussinov, R., & Zhang, J. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00542 · Cited by 355
Kinase-mediated RAS signaling via membraneless cytoplasmic protein granules
Tulpule, A., Guan, J., Neel, D. S., Allegakoen, H. R., Lin, Y. P., Brown, D., Chou, Y.-T., Heslin, A., Chatterjee, N., Perati, S., et al. (2021) · Cell · doi:10.1016/j.cell.2021.03.031 · Cited by 189
Endocytosis and Physiology: Insights from Disabled-2 Deficient Mice
Tao, W., Moore, R., Smith, E. R., & Xu, X.-X. (2016) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2016.00129 · Cited by 43
Metadata
- Authors
- Fehrenbacher, N., Bar-Sagi, D., & Philips, M.
- Venue
- Molecular Oncology
- Publisher
- Wiley
- Published
- 2009-06-26
- Volume
- 3
- Issue
- 4
- Pages
- 297-307
- ISSN
- 1574-7891
- 1878-0261
- PMC
- PMC3003591
- Cited by
- 131
- References
- 3
- Language
- en
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