Phosphotyrosine interaction domain containing 1 (PID1)

Phosphotyrosine interaction domain containing 1 (PID1) is an adaptor protein with a phosphotyrosine-binding (PTB) domain that modulates cell signaling by interacting with proteins such as LRP1. PID1 is implicated in various cellular functions—including negative regulation of insulin signaling and mitochondrial metabolism—in adipocytes and muscle cells. It decreases insulin-stimulated glucose uptake, impairs mitochondrial function, and regulates apoptosis. In cancer biology, especially brain tumors such as medulloblastoma and glioma, PID1 acts as a tumor suppressor by increasing chemotherapy-induced apoptosis, mediated through NF-κB and mitochondrial pathways. Clinically, higher PID1 mRNA levels in these tumors correlate with improved patient survival and greater sensitivity to chemotherapeutic agents like cisplatin and etoposide. PID1 also functions in lipid metabolism, particularly influencing triglyceride-rich lipoprotein uptake[1][2][3][4][6]. Currently, PID1 itself is not considered a direct therapeutic target or receptor, but rather a cell signaling adaptor protein with roles in disease modulation and response to therapy.

Other names

NYGGF4PTB-containing, cubilin and LRP1-interacting proteinPCLI1HMFN2073P-CLI1FLJ20701Protein NYGGF4

Sensitizes tumor cells to chemotherapy-induced apoptosis (mainly via augmenting mitochondrial depolarization and caspase-3 activation)