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The GRB2/Sem‐5 adaptor protein
Abstract
GRB2/Sem‐5 is a 25‐kDa adaptor protein which contains a central Src homology type 2 (SH2) domain flanked by two Src homology type 3 (SH3) domains. GRB2/Sem‐5 was first identified due to the essential role of the sem‐5 gene product in the vulval induction pathway in Caenorhabditis elegans. The SH2 domain of GRB2/Sem‐5 binds to a number of tyrosine phosphorylated proteins, most notably the epidermal growth factor receptor, the insulin receptor substrate IRS‐1 and another putative adaptor protein, She. The SH3 domains bind to Sos, a guanine nucleotide exchange factor for Ras proteins. GRB2/Sem‐5 brings together Sos and tyrosine phosphoproteins into a complex and thereby may regulate the nucleotide exchange rate of Ras and hence its activation state.
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Cited by
A Grb2-associated docking protein in EGF- and insulin-receptor signalling
Holgado-Madruga, M., Emlet, D. R., Moscatello, D. K., Godwin, A. K., & Wong, A. J. (1996) · Nature · doi:10.1038/379560a0 · Cited by 677
Crowley, M. T., Costello, P. S., Fitzer-Attas, C. J., Turner, M., Meng, F., Lowell, C., Tybulewicz, V. L. J., & DeFranco, A. L. (1997) · The Journal of Experimental Medicine · doi:10.1084/jem.186.7.1027 · Cited by 506
Signaling through focal adhesion kinase
Hanks, S. K., & Polte, T. R. (1997) · BioEssays · doi:10.1002/bies.950190208 · Cited by 469
Aronheim, A., Engelberg, D., Li, N., Al-Alawi, N., Schlessinger, J., & Karin, M. (1994) · Cell · doi:10.1016/0092-8674(94)90271-2 · Cited by 458
Ras oncogenes and their downstream targets
Rajalingam, K., Schreck, R., Rapp, U. R., & Albert, Š. (2007) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2007.01.012 · Cited by 458
Metadata
- Authors
- Downward, J.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1994-01-31
- Volume
- 338
- Issue
- 2
- Pages
- 113-117
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2080520906
- Cited by
- 182
- References
- 0
- FWCI
- 6.25
- Type
- journal article
- Language
- en
- Open access
- closed
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