The DOI matches its Crossref record; 49 of the 49 references it cites were found in a registry or an index.
Mechanism for Activation of the EGF Receptor Catalytic Domain by the Juxtamembrane Segment
Open accessAbstract
Signaling by the epidermal growth factor receptor requires an allosteric interaction between the kinase domains of two receptors, whereby one activates the other. We show that the intracellular juxtamembrane segment of the receptor, known to potentiate kinase activity, is able to dimerize the kinase domains. The C-terminal half of the juxtamembrane segment latches the activated kinase domain to the activator, and the N-terminal half of this segment further potentiates dimerization, most likely by forming an antiparallel helical dimer that engages the transmembrane helices of the activated receptor. Our data are consistent with a mechanism in which the extracellular domains block the intrinsic ability of the transmembrane and cytoplasmic domains to dimerize and activate, with ligand binding releasing this block. The formation of the activating juxtamembrane latch is prevented by the C-terminal tails in a new structure of an inactive kinase domain dimer, suggesting how alternative dimers can prevent ligand-independent activation.
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Cites
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An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor
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“Introduction of the L834R mutation, commonly found in lung cancer patients, increases the activity of the kinase core by $14-fold, consistent with previous results (Yun et al., 2007; Zhang et al., 2006) (Figure 2A).”
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Self-citationA Unique Structure for Epidermal Growth Factor Receptor Bound to GW572016 (Lapatinib)
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Cited by
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
Epidermal Growth Factor Receptor Cell Proliferation Signaling Pathways
Wee, P., & Wang, Z. (2017) · Cancers · doi:10.3390/cancers9050052 · Cited by 2,027
Mechanisms of receptor tyrosine kinase activation in cancer
Du, Z., & Lovly, C. M. (2018) · Molecular Cancer · doi:10.1186/s12943-018-0782-4 · Cited by 1,066
The ERBB network: at last, cancer therapy meets systems biology
Yarden, Y., & Pines, G. (2012) · Nature Reviews Cancer · doi:10.1038/nrc3309 · Cited by 988
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Metadata
- Authors
- Jura, N., Endres, N. F., Engel, K., Deindl, S., Das, R., Lamers, M. H., Wemmer, D. E., Zhang, X., & Kuriyan, J.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2009-06
- Volume
- 137
- Issue
- 7
- Pages
- 1293-1307
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2099203391
- Cited by
- 606
- References
- 49
- FWCI
- 20.59
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Jura, N., Endres, N. F., Engel, K., Deindl, S., Das, R., Lamers, M. H., Wemmer, D. E., Zhang, X., & Kuriyan, J. (2009). Mechanism for Activation of the EGF Receptor Catalytic Domain by the Juxtamembrane Segment. Cell. https://doi.org/10.1016/j.cell.2009.04.025
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