Migration and invasion-inhibitory protein (MIIP)

Migration and invasion-inhibitory protein (MIIP) is a cytoplasmic protein encoded by a gene on chromosome 1p36.22, a region often deleted in various cancers. MIIP functions primarily as a tumor suppressor, interacting with IGFBP2 and multiple signaling effectors to inhibit cell proliferation, migration, and invasion in cancer cells. Mechanistically, MIIP regulates protein stability and degradation of key oncogenic mediators such as epidermal growth factor receptor (EGFR) and integrin beta-3 (ITGB3), promoting their proteasomal and lysosomal turnover and inhibiting downstream Ras/MEK/ERK and AKT/β-catenin signaling. MIIP also interferes with HDAC6 and cyclin B1 regulation and attenuates angiogenesis by reducing VEGFA production and blocking epithelial-mesenchymal transition (EMT). Prognostically, high MIIP expression associates with improved survival in certain cancers, including non-small cell lung cancer and triple-negative breast cancer patients. MIIP is under investigation as a potential diagnostic and therapeutic biomarker, although its effects may vary according to cancer type and molecular context.

Other names

MIIPIIP45IIp45FLJ12438IGFBP2-binding proteinInvasion-inhibitory protein 45

Drugs (potential or investigational) targeting MIIP would likely act through upregulation or mimicking of MIIP activity, promoting proteasomal and lysosomal degradation of EGFR and inhibiting ITGB3-mediated angiogenic signaling cascades