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An Alternative to SH2 Domains for Binding Tyrosine-Phosphorylated Proteins
Abstract
Src homology 2 (SH2) domains bind specifically to tyrosine-phosphorylated proteins that participate in signaling by growth factors and oncogenes. A protein domain was identified that bound specifically to the tyrosine-phosphorylated form of its target protein but differs from known SH2 sequences. Phosphotyrosine-binding (PTB) domains were found in two proteins: SHC, a protein implicated in signaling through Ras; and SCK, encoded by a previously uncharacterized gene. The PTB domain of SHC specifically bound to a tyrosine-phosphorylated 145-kilodalton protein. PTB domains are an alternative to SH2 domains for specifically recruiting tyrosine-phosphorylated proteins into signaling complexes and are likely to take part in signaling by many growth factors.
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Saxton, T. M., van Oostveen, I., Bowtell, D., Aebersold, R., & Gold, M. R. (1994) · The Journal of Immunology · doi:10.4049/jimmunol.153.2.623 · Cited by 164
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Pawson, T., & Scott, J. D. (1997) · Science · doi:10.1126/science.278.5346.2075 · Cited by 2,256
The IL-4 receptor: signaling mechanisms and biologic functions
Nelms, K., Keegan, A. D., Zamorano, J., Ryan, J. J., & Paul, W. E. (1999) · Annual Review of Immunology · doi:10.1146/annurev.immunol.17.1.701 · Cited by 1,545
TrkB signalling pathways in LTP and learning
Minichiello, L. (2009) · Nature Reviews Neuroscience · doi:10.1038/nrn2738 · Cited by 1,055
Kouhara, H., Hadari, Y. R., Spivak-Kroizman, T., Schilling, J., Bar-Sagi, D., Lax, I., & Schlessinger, J. (1997) · Cell · doi:10.1016/s0092-8674(00)80252-4 · Cited by 873
Metadata
- Authors
- Kavanaugh, W. M., & Williams, L. T.
- Venue
- Science
- Published
- 1994-12-16
- Volume
- 266
- Issue
- 5192
- Pages
- 1862-1865
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1997859241
- Cited by
- 501
- References
- 1
- FWCI
- 24.88
- Type
- journal article
- Language
- en
- Open access
- closed
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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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