title: Microtubule plus-ends within a mitotic cell are 'moving platforms' with anchoring, signalling and force-coupling roles.
abstract: The microtubule polymer grows and shrinks predominantly from one of its ends called the 'plus-end'. Plus-end regulation during interphase is well understood. However, mitotic regulation of plus-ends is only beginning to be understood in mammalian cells. During mitosis, the plus-ends are tethered to specialized microtubule capture sites. At these sites, plus-end-binding proteins are loaded and unloaded in a regulated fashion. Proper tethering of plus-ends to specialized sites is important so that the microtubule is able to translate its growth and shrinkage into pushing and pulling forces that move bulky subcellular structures. We discuss recent advances on how mitotic plus-ends are tethered to distinct subcellular sites and how plus-end-bound proteins can modulate the forces that move subcellular structures. Using end binding 1 (EB1) as a prototype plus-end-binding protein, we highlight the complex network of plus-end-binding proteins and their regulation through phosphorylation. Finally, we develop a speculative 'moving platform' model that illustrates the plus-end's role in distinguishing correct versus incorrect microtubule interactions.
authors.affiliation: Department of Genetics, University of Cambridge, Downing Site, Downing Street, Cambridge CB2 3EH, UK.
authors.forename: Naoka
authors.initials: N
authors.lastname: Tamura
authors.forename: Viji M
authors.initials: VM
authors.lastname: Draviam
mesh_terms: D000818:Animals; D005057:Eukaryotic Cells / Q000502:physiology*; D005786:Gene Expression Regulation; D007399:Interphase / Q000502:physiology; D018386:Kinetochores / Q000502:physiology; D008869:Microtubule-Associated Proteins / Q000235:genetics / Q000378:metabolism*; D008870:Microtubules / Q000502:physiology*; D008938:Mitosis / Q000502:physiology*; D010766:Phosphorylation; D011485:Protein Binding; D015398:Signal Transduction
chemical_list: D008869:Microtubule-Associated Proteins