Function

Stathmin (STM) regulates microtubules dynamics. Microtubules undergo continuous assembly and disassembly in the cell’s cytoskeleton. STM binds to tubulin and prevents the latter from polymerization thus preventing microtubule assembly. Phosphorylation of STM weakens the binding of STM to tubulin enabling the microtubule assembly needed for the formation of mitotic spindle. Thus, STM is an oncoprotein. STM contains an SLD (Stathmin-Like Domain) domain of 149 residues which binds the tubulin dimer[1].

Disease

Decreased levels of STM are found in brains of adults with Down syndrome and Alzheimer disease[2].

Relevance

Structural highlights

Rat stathmin SLD domain (magenta) complex with tubulin α chain (grey, pink), tubulin β chain (green, yellow), GTP, sulfate and Mg+2 ions (PDB code 3ryf)

Drag the structure with the mouse to rotate

3D Structures of stathmin3D Structures of stathmin

Updated on 01-September-2016

ReferencesReferences

  1. Curmi PA, Gavet O, Charbaut E, Ozon S, Lachkar-Colmerauer S, Manceau V, Siavoshian S, Maucuer A, Sobel A. Stathmin and its phosphoprotein family: general properties, biochemical and functional interaction with tubulin. Cell Struct Funct. 1999 Oct;24(5):345-57. PMID:15216892
  2. Cheon MS, Fountoulakis M, Cairns NJ, Dierssen M, Herkner K, Lubec G. Decreased protein levels of stathmin in adult brains with Down syndrome and Alzheimer's disease. J Neural Transm Suppl. 2001;(61):281-8. PMID:11771751

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Joel L. Sussman