title: Encoding the microtubule structure: Allosteric interactions between the microtubule +TIP complex master regulators and TOG-domain proteins.
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.
authors.affiliation: a Department of Cell and Developmental Biology ; Vanderbilt University Medical Center ; Nashville , TN USA.
authors.forename: Ashley D
authors.initials: AD
authors.lastname: Grimaldi
authors.forename: Marija
authors.initials: M
authors.lastname: Zanic
authors.forename: Irina
authors.initials: I
authors.lastname: Kaverina
mesh_terms: D000818:Animals; D018797:Cell Cycle Proteins / Q000378:metabolism; D006801:Humans; D008869:Microtubule-Associated Proteins / Q000737:chemistry / Q000378:metabolism*; D008870:Microtubules / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D015398:Signal Transduction; D013329:Structure-Activity Relationship; D029867:Xenopus Proteins / Q000378:metabolism
chemical_list: C486738:CKAP5 protein, Xenopus; C509362:CLASP1 protein, Xenopus; D018797:Cell Cycle Proteins; D008869:Microtubule-Associated Proteins; D029867:Xenopus Proteins
keywords: CLASP; XMAP215; cytoskeleton; end-binding proteins; microtubule dynamics; microtubules