[The stathmin-tubulin interaction and the regulation of the microtubule assembly].
Stathmin family proteins interact with tubulin and negatively regulate its assembly in microtubules. One stathmin molecule forms a complex with two alphabeta tubulin heterodimers in an interaction that is weakened upon stathmin phosphorylation. The X-ray structure of crystals of the complex reveals a head-to-tail arrangement of the two tubulins which are connected by a long stathmin alpha helix. By holding tubulins in a curved complex that is not incorporated in microtubules, stathmin lowers the pool of "assembly competent" tubulin. An alternate mechanism has been also proposed to account for the stathmin action in vivo; it involves a direct interaction of stathmin with microtubule (+) ends. More experiments are needed to evaluate the relative contribution of this alternative mechanism to the regulation of tubulin assembly by stathmin.
Gigant
B
B
Laboratoire d'Enzymologie et Biochimie Structurales, UPR 9063, Centre National de la Recherche Scientifique, Bâtiment 34, 1, avenue de la Terrasse, 91198 cedex, Gif-sur-Yvette, France. gigant@lebs.cnrs-gif.fr
Martin-Barbey
C
C
Curmi
P A
PA
Sobel
A
A
Knossow
M
M
D019281:Dimerization; D008868:Microtubule Proteins; D008870:Microtubules / Q000737:chemistry* / Q000648:ultrastructure; D008958:Models, Molecular; D010750:Phosphoproteins / Q000378:metabolism*; D010766:Phosphorylation; D017433:Protein Structure, Secondary; D050777:Stathmin; D014404:Tubulin / Q000378:metabolism*
D008868:Microtubule Proteins; D010750:Phosphoproteins; D050777:Stathmin; D014404:Tubulin