The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
IRS-1 is a common element in insulin and insulin-like growth factor-I signaling to the phosphatidylinositol 3'-kinase
Abstract
IRS-1 is a unique cytosolic protein that becomes tyrosine phosphorylated during insulin stimulation of intact cells and immediately associates with the phosphatidylinositol 3'-kinase (PtdIns 3'-kinase). The insulin-like growth factor-I (IGF-I) receptor also mediated the tyrosine phosphorylation of IRS-1 and increased the amount of PtdIns 3'-kinase activity bound to IRS-1 in Chinese hamster ovary cells. Purified insulin receptor and IGF-I receptor phosphorylated recombinant baculovirus-produced IRS-1 on similar sites in vitro, and phosphorylated baculovirus-produced IRS-1 bound PtdIns 3'-kinase activity from lysates of quiescent cells. Treatment of cells with IGF-I activated the PtdIns 3'-kinase, suggesting that IGF-I activates the PtdIns 3'-kinase through IRS-1 binding to p85 in a manner similar to insulin. Chinese hamster ovary cells overexpressing IRS-1 demonstrated increased tyrosine phosphorylation of IRS-1, and more PtdIns 3'-kinase activity associated with IRS-1 in these cells. These data demonstrate that IRS-1 is a common element for signal transmission by the IGF-I and insulin receptors.
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Citations
Cites
Structure of the insulin receptor substrate IRS-1 defines a unique signal transduction protein
Sun, X. J., Rothenberg, P., Kahn, C. R., Backer, J. M., Araki, E., Wilden, P. A., Cahill, D. A., Goldstein, B. J., & White, M. F. (1991) · Nature · doi:10.1038/352073a0 · Cited by 1,574
Self-citationExpression and function of IRS-1 in insulin signal transmission.
Sun, X. J., Miralpeix, M., Myers, M. G., Glasheen, E. M., Backer, J. M., Kahn, C. R., & White, M. F. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)41723-1 · Cited by 326
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Cited by
Alternative pathway of insulin signalling in mice with targeted disruption of the IRS-1 gene
Araki, E., Lipes, M. A., Patti, M.-E., Brüning, J. C., Haag III, B., Johnson, R. S., & Kahn, C. R. (1994) · Nature · doi:10.1038/372186a0 · Cited by 1,252
Growth Hormone, Insulin-Like Growth Factors, and the Skeleton
Giustina, A., Mazziotti, G., & Canalis, E. (2008) · Endocrine Reviews · doi:10.1210/er.2007-0036 · Cited by 914
Svegliati-Baroni, G., Ridolfi, F., Di Sario, A., Casini, A., Marucci, L., Gaggiotti, G., Orlandoni, P., Macarri, G., Perego, L., Benedetti, A., et al. (1999) · Hepatology · doi:10.1002/hep.510290632 · Cited by 320
De Meyts, P. (1994) · Diabetologia · doi:10.1007/bf00400837 · Cited by 285
Zheng, W., & Quirion, R. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02350.x · Cited by 225
Metadata
- Authors
- Myers, M. G.
- Venue
- Endocrinology
- Publisher
- The Endocrine Society
- Published
- 1993-04-01
- Volume
- 132
- Issue
- 4
- Pages
- 1421-1430
- ISSN
- 0013-7227 (ISSN-L)
- OpenAlex
- W2031938665
- Cited by
- 333
- References
- 2
- FWCI
- 10.74
- Type
- journal article
- Language
- en
- Open access
- closed
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- Myers, M. G. (1993). IRS-1 is a common element in insulin and insulin-like growth factor-I signaling to the phosphatidylinositol 3'-kinase. Endocrinology. https://doi.org/10.1210/en.132.4.1421
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