title: Cytoskeleton: what does GTP do for septins?
abstract: The recent observation of GTP-promoted polymerization of a single septin polypeptide suggests that this protein has tubulin-like biochemical properties. This model cannot, however, explain the GTP-biochemistry of heteromeric septin complexes from cytosol.
authors.affiliation: Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115-5731, USA.
authors.forename: Timothy J
authors.initials: TJ
authors.lastname: Mitchison
authors.forename: Christine M
authors.initials: CM
authors.lastname: Field
mesh_terms: D000818:Animals; D003599:Cytoskeleton / Q000502:physiology*; D019204:GTP-Binding Proteins / Q000378:metabolism*; D006160:Guanosine Triphosphate / Q000378:metabolism*; D008322:Mammals; D017510:Protein Folding; D011994:Recombinant Proteins / Q000378:metabolism
chemical_list: D011994:Recombinant Proteins; D006160:Guanosine Triphosphate; D019204:GTP-Binding Proteins