Structure and thermodynamics of the tubulin-stathmin interaction

J Struct Biol. 2007 May;158(2):137-47. doi: 10.1016/j.jsb.2006.07.018. Epub 2006 Aug 23.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Humans
  • Molecular Sequence Data
  • Phosphorylation
  • Protein Structure, Secondary
  • Stathmin / chemistry*
  • Stathmin / ultrastructure*
  • Thermodynamics
  • Tubulin / chemistry*
  • Tubulin / ultrastructure*

Substances

  • Stathmin
  • Tubulin