Encoding the microtubule structure: Allosteric interactions between the microtubule +TIP complex master regulators and TOG-domain proteins.
AUTHORS
Grimaldi| Zanic| Kaverina
AD| M| IAshley D| Marija| Irina .
Cell cycle (Georgetown, Tex.). 2015 ; 14(9).
1375-8
- PMID: 25895033[PubMed].
ABSTRACT
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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