title: Visualizing microtubule structural transitions and interactions with associated proteins.
abstract: Microtubules (MTs) have been the subject of cryo-electron microscopy (cryo-EM) studies since the birth of this technique. Although MTs pose some unique challenges, having to do with the presence of a MT seam, lattice variability and disorder, MT cryo-EM reconstructions are steadily improving in resolution and providing exciting new insights into MT structure and function. Recent work has lead to the atomic-detail visualization of lateral contacts between tubulin subunits and the conformational changes that give rise to strain in the MT lattice accompanying GTP hydrolysis. Cryo-EM has also been invaluable in describing the interactions between MTs and MT associated proteins (MAPs), which function to regulate MT dynamic instability, move cargoes, or contribute to other MT cellular processes.
authors.affiliation: Molecular and Cell Biology Department and QB3 Institute, UC Berkeley, CA 94720, United States; Howard Hughes Medical Institute, UC Berkeley, CA 94720, United States; Molecular Biophysics and Integrative Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, United States. Electronic address: enogales@lbl.gov.
authors.forename: Eva
authors.initials: E
authors.lastname: Nogales
authors.affiliation: Howard Hughes Medical Institute, UC Berkeley, CA 94720, United States; Molecular Biophysics and Integrative Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, United States.
authors.forename: Rui
authors.initials: R
authors.lastname: Zhang
mesh_terms: D020285:Cryoelectron Microscopy; D008870:Microtubules / Q000737:chemistry*; D011485:Protein Binding; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*
chemical_list: D011506:Proteins