title: Promoting microtubule assembly: A hypothesis for the functional significance of the +TIP network.
abstract: Regulation of microtubule (MT) dynamics is essential for many cellular processes, but the machinery that controls MT dynamics remains poorly understood. MT plus-end tracking proteins (+TIPs) are a set of MT-associated proteins that dynamically track growing MT ends and are uniquely positioned to govern MT dynamics. +TIPs associate with each other in a complex array of inter- and intra-molecular interactions known as the "+TIP network." Why do so many +TIPs bind to other +TIPs? Typical answers include the ideas that these interactions localize proteins where they are needed, deliver proteins to the cortex, and/or create regulatory pathways. We propose an additional and more mechanistic hypothesis: that +TIPs bind each other to create a superstructure that promotes MT assembly by constraining the structural fluctuations of the MT tip, thus acting as a polymerization chaperone.
authors.affiliation: Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN, USA.
authors.forename: Kamlesh K
authors.initials: KK
authors.lastname: Gupta
authors.forename: Emily O
authors.initials: EO
authors.lastname: Alberico
authors.forename: Inke S
authors.initials: IS
authors.lastname: Näthke
authors.forename: Holly V
authors.initials: HV
authors.lastname: Goodson
mesh_terms: D000818:Animals; D006801:Humans; D008869:Microtubule-Associated Proteins / Q000378:metabolism*; D008870:Microtubules / Q000378:metabolism*; D018832:Molecular Chaperones / Q000378:metabolism; D060066:Protein Interaction Maps; D055503:Protein Multimerization
chemical_list: D008869:Microtubule-Associated Proteins; D018832:Molecular Chaperones
keywords: APC; CLIP-170; EB1; light scattering assay; microtubule bundling; polymerization chaperone