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Rho family-interacting cell polarization regulator 1 (RIPOR1) is an adapter and scaffold protein that directly binds active RHO GTPases (notably RHOA, RHOB, and RHOC) through a conserved N-terminal RHO-binding motif, thereby negatively regulating their activity. This action is crucial for directing cell polarity and migration, including Golgi apparatus reorientation in response to external stimuli and wounding. RIPOR1’s functions are mediated through protein-protein interactions, especially in linking RHO GTPases to Golgi-localizing proteins. Its expression is widespread across tissues, and dysregulation has been implicated contextually in cancer and immune cell migration, with emerging evidence supporting broader disease relevance. While it is not classified as a classical receptor or enzyme, it plays a vital role in cellular signaling networks involving the actin cytoskeleton and directional movement. No clinically approved drugs directly target RIPOR1, and its utility as a biomarker is presently investigational.
Scaffold/adapter function modulating RHO GTPase activity through direct binding. Influences Golgi reorientation and cell migration by bridging RHO GTPases to Golgi-localizing partners
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