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Interaction of Shc with the ζ Chain of the T Cell Receptor Upon T Cell Activation
Abstract
The shc oncogene product is tyrosine-phosphorylated by Src family kinases and after its phosphorylation interacts with the adapter protein Grb2 (growth factor receptor-bound protein 2). In turn, Grb2 interacts with the guanine nucleotide exchange factor for Ras, mSOS. Because several Src family kinases participate in T cell activation and Shc functions upstream of Ras, the role of Shc in T cell signaling was examined. Shc was phosphorylated on tyrosine after activation through the T cell receptor (TCR), and subsequently interacted with Grb2 and mSOS. The Src homology region 2 (SH2) domain of Shc directly interacted with the tyrosine-phosphorylated ζ chain of the TCR. Thus, Shc may couple TCR activation to the Ras signaling pathway.
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Cited by
Regulation of T Cell Receptor Signaling by Tyrosine Phosphatase SYP Association with CTLA-4
Marengère, L. E. M., Waterhouse, P., Duncan, G. S., Mittrücker, H.-W., Feng, G.-S., & Mak, T. W. (1996) · Science · doi:10.1126/science.272.5265.1170 · Cited by 551
Helgason, C. D., Damen, J. E., Rosten, P., Grewal, R., Sorensen, P., Chappel, S. M., Borowski, A., Jirik, F., Krystal, G., & Humphries, R. K. (1998) · Genes & Development · doi:10.1101/gad.12.11.1610 · Cited by 556
Lamkin, T. D., Walk, S. F., Liu, L., Damen, J. E., Krystal, G., & Ravichandran, K. S. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.16.10396 · Cited by 118
Self-citationWare, M., Rosten, P., Damen, J., Liu, L., Humphries, R., & Krystal, G. (1996) · Blood · doi:10.1182/blood.v88.8.2833.bloodjournal8882833 · Cited by 96
Yablonski, D. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.01704 · Cited by 53
Dave, V. (1998) · International Immunology · doi:10.1093/intimm/10.10.1481 · Cited by 8
Metadata
- Authors
- Ravichandran, K. S., Lee, K. K., Songyang, Z., Cantley, L. C., Burn, P., & Burakoff, S. J.
- Venue
- Science
- Published
- 1993-11-05
- Volume
- 262
- Issue
- 5135
- Pages
- 902-905
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2001467625
- Cited by
- 330
- References
- 0
- FWCI
- 18.86
- Type
- journal article
- Language
- en
- Open access
- closed
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