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STMN1  -  stathmin 1

Bos taurus

 
 
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High impact information on STMN1

  • Phosphoproteins of the stathmin family interact with the alphabeta tubulin heterodimer (tubulin) and hence interfere with microtubule dynamics [1].
  • We propose that stathmin acts solely by sequestering tubulin, without affecting microtubule dynamics, and that the effect of stathmin phosphorylation on microtubule assembly depends on tubulin critical concentration [2].
  • Stathmin is a highly conserved ubiquitous cytoplasmic protein, phosphorylated in response to extracellular signals and during the cell cycle [3].
  • Stathmin slows down guanosine diphosphate dissociation from tubulin in a phosphorylation-controlled fashion [4].
  • At molar ratios of stathmin to tubulin lower than 0.5, biphasic kinetics were observed, indicating that the dynamics of the complex is extremely slow, consistent with its high stability [4].
 

Biological context of STMN1

 

Associations of STMN1 with chemical compounds

  • The serine-to-glutamate substitution of all four phosphorylatable serines of stathmin (4E-stathmin) weakens the stability of the T(2)S complex by about 2 orders of magnitude [4].
 

Physical interactions of STMN1

  • In this study we have used limited proteolysis and cross-linking analysis to localize further the stathmin-binding site on alpha-tubulin [5].
 

Analytical, diagnostic and therapeutic context of STMN1

References

  1. The 4 A X-ray structure of a tubulin:stathmin-like domain complex. Gigant, B., Curmi, P.A., Martin-Barbey, C., Charbaut, E., Lachkar, S., Lebeau, L., Siavoshian, S., Sobel, A., Knossow, M. Cell (2000) [Pubmed]
  2. The effect of stathmin phosphorylation on microtubule assembly depends on tubulin critical concentration. Amayed, P., Pantaloni, D., Carlier, M.F. J. Biol. Chem. (2002) [Pubmed]
  3. The stathmin/tubulin interaction in vitro. Curmi, P.A., Andersen, S.S., Lachkar, S., Gavet, O., Karsenti, E., Knossow, M., Sobel, A. J. Biol. Chem. (1997) [Pubmed]
  4. Stathmin slows down guanosine diphosphate dissociation from tubulin in a phosphorylation-controlled fashion. Amayed, P., Carlier, M.F., Pantaloni, D. Biochemistry (2000) [Pubmed]
  5. OP18/stathmin binds near the C-terminus of tubulin and facilitates GTP binding. Moreno, F.J., Bagnat, M., Lim, F., Avila, J. Eur. J. Biochem. (1999) [Pubmed]
  6. Stathmin strongly increases the minus end catastrophe frequency and induces rapid treadmilling of bovine brain microtubules at steady state in vitro. Manna, T., Thrower, D., Miller, H.P., Curmi, P., Wilson, L. J. Biol. Chem. (2006) [Pubmed]
 
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