Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
XB-ART-53265
Cell Cycle January 1, 2015; 14 (9): 1375-8.

Encoding the microtubule structure: Allosteric interactions between the microtubule +TIP complex master regulators and TOG-domain proteins.

Grimaldi AD , Zanic M , Kaverina I .


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.

PubMed ID: 25895033
PMC ID: PMC4614873
Article link: Cell Cycle
Grant support: [+]
Genes referenced: ckap5

References [+] :
Akhmanova, Tracking the ends: a dynamic protein network controls the fate of microtubule tips. 2008, Pubmed


Xenbase: The Xenopus Model Organism Knowledgebase.
Version: 4.14.0
Major funding for Xenbase is provided by grant P41 HD064556