β₁-integrin controls IGF-1R internalization and intracellular signaling.

ABSTRACT: Cell adhesion-dependent phosphorylation of insulin-like growth factor 1 receptor (IGF-1R) on its C-terminal tail (CT) at Tyr^1250/1251 promotes receptor internalization and Golgi accumulation. We previously proposed that this phosphorylation is associated with cell migration and cancer aggressiveness, distinguishing IGF-1R activity from that of insulin receptor, which lacks these tyrosines. Here, we further investigated how adhesion signaling influences IGF-1R location and activity in migratory cancer cells and R- fibroblasts. We observed that IGF-1R, in triple-negative breast cancer tissues, is predominantly intracellular and dispersed from the plasma membrane compared with nontumor tissue. Datasets from basal-like breast cancer patients indicated a strong, positive correlation

SUBMITTER: McDermott N 

PROVIDER: S-EPMC11732470 | biostudies-literature | 2025 Jan

REPOSITORIES: biostudies-literature