Migration and invasion inhibitory protein (MIIP) (MIIP)

Migration and invasion inhibitory protein (MIIP), also known as IIP45, is a 45 kDa protein that functions as a potent tumor suppressor by regulating the cytoskeleton and cell cycle progression [1][2]. It exerts its primary biological effect by binding to and inhibiting histone deacetylase 6 (HDAC6), which leads to increased acetylation of alpha-tubulin and altered microtubule dynamics, effectively reducing the migratory and invasive capacity of cancer cells [3]. Additionally, MIIP interacts with insulin-like growth factor binding protein 2 (IGFBP2), sequestering it and preventing its pro-tumorigenic and pro-angiogenic signaling pathways [4]. In clinical contexts, MIIP is frequently downregulated in various malignancies, including high-grade gliomas and breast carcinomas, where its low expression serves as a biomarker for poor prognosis and increased metastatic potential [5]. While there are currently no FDA-approved drugs specifically targeting MIIP, it is an active area of research for mRNA-based therapeutic restoration and gene therapy [6]. By delivering MIIP mRNA to deficient tumor cells, researchers aim to reinstate its inhibitory control over cell invasion and mitosis, providing a potential strategy to combat aggressive and metastatic cancers [3][5].

Other names

IIP45Invasion inhibitory protein 45IGFBP2-binding proteinMigration and invasion-inhibitory protein

Restoration of tumor suppressor function through the delivery of functional mRNA to increase MIIP protein levels, which subsequently inhibits HDAC6 activity and IGFBP2 signaling to suppress tumor cell motility and proliferation [1][3].