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Since their initial discovery, the intriguing proteins of the +TIP network have been the focus of intense investigation. Although many of the individual +TIP functions have been revealed, the capacity for +TIP proteins to regulate each other has not been widely addressed. Importantly, recent studies involving EBs, the master regulators of the +TIP complex, and several TOG-domain proteins have uncovered a novel mechanism of mutual +TIP regulation: allosteric interactions through changes in microtubule structure. These findings have added another level of complexity to the existing evidence on +TIP regulation and highlight the cooperative nature of the +TIP protein network.
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