IGFR

IGFR stands for Insulin-like Growth Factor Receptor. It is a transmembrane receptor protein that plays a crucial role in cellular growth, proliferation, and survival. The IGFR is activated by binding to insulin-like growth factors, primarily IGF-1 and IGF-2. This binding triggers a cascade of intracellular signaling pathways, including the PI3K/Akt pathway and the MAPK pathway, which ultimately influence gene expression and cellular processes.

The IGFR is composed of two extracellular alpha subunits and two transmembrane beta subunits, linked together by disulfide bonds. When IGFs bind to the alpha subunits, they induce a conformational change that activates the intracellular tyrosine kinase domain of the beta subunits. This autophosphorylation is the first step in transducing the signal into the cell.

Dysregulation of IGFR signaling has been implicated in a variety of diseases, including cancer and diabetes. In many cancers, IGFR is overexpressed or mutated, contributing to uncontrolled cell growth and resistance to apoptosis. Conversely, impaired IGFR signaling can lead to growth deficiencies. Research into IGFR is ongoing, aiming to understand its complex roles in normal physiology and disease, and to develop targeted therapies.