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MIIP, a Cytoskeleton Regulator that Blocks Cell Migration and Invasion, Delays Mitosis, and Suppresses Tumorogenesis

[ Vol. 12 , Issue. 1 ]


Wei Zhang, Jing Wen and Yingmei Wang   Pages 68 - 73 ( 6 )


The migration and invasion inhibitory protein (MIIP) was initially discovered in a yeast two-hybrid screen for proteins that interact and inhibit the migration and invasion – promoting protein insulin-like growth factor binding protein 2 (IGFBP2). Recent studies have shown that MIIP not only modulates IGFBP2 but also regulates microtubule by binding to and inhibiting HDAC6, a class 2 histone deacetylase that deacetylates -tubulin, heat-shock protein 90 (HSP90), and cortactin. In addition, MIIP also regulates the mitosis checkpoint, another microtubule-associated process. The location of the MIIP gene in chromosomal region 1p36, a commonly deleted region in a broad spectrum of human cancers, and the observation that MIIP attenuates tumorigenesis in a mouse model suggest that it functions as a tumor-suppressor gene. This review summarizes the recent progress in characterizing this novel protein, which regulates cell migration and mitosis, two processes that rely on the highly coordinated dynamics of the microtubule and cytoskeleton systems.


mitosis, cell motility, tumor-suppressor gene, MIIP


Department of Pathology, Unit 85, The University of Texas MD Anderson Cancer Center, 1515 HolcombeBlvd., Houston, TX 77030, USA.

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