Related Experiment Video
Updated: Aug 29, 2026

Coculture Analysis of Extracellular Protein Interactions Affecting Insulin Secretion by Pancreatic Beta Cells
Published on: June 15, 2013
The expression of Sam68, a protein involved in insulin signal transduction, is enhanced by insulin stimulation
V Sánchez-Margalet1, C González-Yanes, S Najib
1Department of Medical Biochemistry and Molecular Biology, Medical School, Investigation Unit, Virgen Macarena University Hospital, Av. Sanchez Pizjuan 4, Seville 41009, Spain. margalet@us.es
Abstract:
The role of Sam68, an RNA binding protein and putative substrate of the insulin receptor (IR) in insulin signaling was studied using CHO wild type (WT) cells, CHO cells overexpressing IR, and rat white adipocytes as a physiological system. In CHO-IR cells and adipocytes, Sam68 was tyrosine phosphorylated in response to insulin, and then associated with p85 phosphatidylinositol-3 kinase along with IRS-1. Sam68 was localized mainly in the nucleus of CHO-WT, and both in the nucleus and cytoplasm of CHO-IR cells, but only in the cytoplasm of rat white adipocytes. Insulin stimulation for 16 h enhanced the expression of Sam68 in rat adipocytes and CHO-IR cells. Moreover, CHO-IR cells expressed more Sam68 than CHO-WT, suggesting that overexpression of the IR is enough to induce the expression of Sam68. In summary, these results demonstrate that Sam68 works as a cytoplasmic docking protein which is recruited by IR signaling and whose expression is induced by insulin stimulation, suggesting a putative role for Sam68 in insulin signal transduction.
Related Concept Videos
Cell Specific Gene Expression
Insulin Secretory Vesicles
PI3K/mTOR/AKT Signaling Pathway
Hormones Regulating Blood Glucose
In addition to accelerating glucose uptake and utilization, insulin has...
Glucose Homeostasis: Pancreatic Islets and Insulin Secretion
Insulin and C-peptide are co-secreted in...
Insulin: The Receptor and Signaling Pathways

