title: Structure and thermodynamics of the tubulin-stathmin interaction.
abstract: Oncoprotein 18/stathmin (stathmin) is a phosphorylation-controlled key regulator of microtubule dynamics. In recent years, substantial efforts were undertaken to characterize the complex formed between tubulin and the intrinsically disordered stathmin molecule. Here, I summarize and illustrate the current structural and thermodynamic studies on the tubulin-stathmin interaction. Based on these and on functional information I formulate an updated molecular mechanism on how tubulin-binding by stathmin regulates microtubule dynamics.
authors.affiliation: Biomolecular Research, Structural Biology, Paul Scherrer Institut, CH-5232 Villigen PSI, Switzerland. michel.steinmetz@psi.ch
authors.forename: Michel O
authors.initials: MO
authors.lastname: Steinmetz
mesh_terms: D000595:Amino Acid Sequence; D006801:Humans; D008969:Molecular Sequence Data; D010766:Phosphorylation; D017433:Protein Structure, Secondary; D050777:Stathmin / Q000737:chemistry* / Q000648:ultrastructure*; D013816:Thermodynamics; D014404:Tubulin / Q000737:chemistry* / Q000648:ultrastructure*
chemical_list: D050777:Stathmin; D014404:Tubulin