| Autor: |
Baron V; Institut National de la Santé et de la Recherche Médicale U145, Faculté de Médecine, Nice, France., Alengrin F, Van Obberghen E |
| Jazyk: |
angličtina |
| Zdroj: |
Endocrinology [Endocrinology] 1998 Jun; Vol. 139 (6), pp. 3034-7. |
| DOI: |
10.1210/endo.139.6.6131 |
| Abstrakt: |
The activated insulin receptor phosphorylates docking proteins such as Src-Homology Collagen (Shc) and Insulin Receptor Substrate-1 (IRS-1), which then bind several proteins that contain a Src-Homology 2 (SH2) domain. Both Shc and IRS-1 associate with Growth Factor Receptor-Bound protein 2 (Grb2), an adaptor molecule. The hormone-receptor complex is then rapidly internalized through coated-pits. Dynamin, a 100 kDa protein with GTPase activity, is thought to play a crucial role in receptor-mediated endocytosis. In this study, we show that insulin induces tyrosine phosphorylation of dynamin in cells overexpressing human insulin receptors. Phosphorylation is observed rapidly, i.e. within 1 minute of insulin treatment. Moreover, exposure of cells to the hormone leads to co-immunoprecipitation of dynamin with Shc and with insulin receptor. Since dynamin constitutively associates with Grb2, it could be recruited to the insulin signaling complex through binding of Grb2 to tyrosine-phosphorylated Shc. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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