The DOI matches its Crossref record; 240 of the 240 references it cites were found in a registry or an index.
Endocytosis of Receptor Tyrosine Kinases
Open accessAbstract
Endocytosis is the major regulator of signaling from receptor tyrosine kinases (RTKs). The canonical model of RTK endocytosis involves rapid internalization of an RTK activated by ligand binding at the cell surface and subsequent sorting of internalized ligand-RTK complexes to lysosomes for degradation. Activation of the intrinsic tyrosine kinase activity of RTKs results in autophosphorylation, which is mechanistically coupled to the recruitment of adaptor proteins and conjugation of ubiquitin to RTKs. Ubiquitination serves to mediate interactions of RTKs with sorting machineries both at the cell surface and on endosomes. The pathways and kinetics of RTK endocytic trafficking, molecular mechanisms underlying sorting processes, and examples of deviations from the standard trafficking itinerary in the RTK family are discussed in this work.
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Cell Signaling by Receptor Tyrosine Kinases
Lemmon, M. A., & Schlessinger, J. (2010) · Cell · doi:10.1016/j.cell.2010.06.011 · Cited by 7,929
Untangling the ErbB signalling network
Yarden, Y., & Sliwkowski, M. X. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35052073 · Cited by 6,974
Rab proteins as membrane organizers
Zerial, M., & McBride, H. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35052055 · Cited by 3,381
Cantley, L. C., & Neel, B. G. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.8.4240 · Cited by 2,006
Anderson, R. G. W. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.199 · Cited by 1,942
GROWTH FACTOR RECEPTOR TYROSINE KINASES
Yarden, Y., & Ullrich, A. (1988) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.57.070188.002303 · Cited by 1,838
BAR Domains as Sensors of Membrane Curvature: The Amphiphysin BAR Structure
Peter, B. J., Kent, H. M., Mills, I. G., Vallis, Y., Butler, P. J. G., Evans, P. R., & McMahon, H. T. (2004) · Science · doi:10.1126/science.1092586 · Cited by 1,636
The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signaling
Lowenstein, E. J., Daly, R. J., Batzer, A. G., Li, W., Margolis, B., Lammers, R., Ullrich, A., Skolnik, E. Y., Bar-Sagi, D., & Schlessinger, J. (1992) · Cell · doi:10.1016/0092-8674(92)90167-b · Cited by 1,631
Henne, W. M., Buchkovich, N. J., & Emr, S. D. (2011) · Developmental Cell · doi:10.1016/j.devcel.2011.05.015 · Cited by 1,496
Katzmann, D. J., Babst, M., & Emr, S. D. (2001) · Cell · doi:10.1016/s0092-8674(01)00434-2 · Cited by 1,429
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Endocytosis in the context-dependent regulation of individual and collective cell properties
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Metadata
- Authors
- Goh, L. K., & Sorkin, A.
- Venue
- Cold Spring Harbor Perspectives in Biology
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2013-05-01
- Volume
- 5
- Issue
- 5
- Pages
- a017459-a017459
- ISSN
- 1943-0264 (ISSN-L)
- OpenAlex
- W2119748249
- Cited by
- 461
- References
- 240
- Type
- posted content
- Language
- en
- Open access
- bronze
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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