InterPro domain: IPR036002

Stathmin [ 1 ] (from the Greek 'stathmos' which means relay), is a ubiquitous intracellular protein, present in a variety of phosphorylated forms. It is involved in the regulation of the microtubule (MT) filament system by destabilising microtubules. It prevents assembly and promotes disassembly of microtubules [ 2 ]. However, when phosphorylated, its destabilisation ability is significantly reduced [ 3 ].

The stathmin family also includes:

• Stathmin 2 (Protein SCG10); a neuron-specific, membrane-associated protein that accumulates in the growth cones of developing neurons. It is highly similar in its sequence to stathmin, but differs in that it contains an additional N-terminal hydrophobic segment of 32 residues which is probably responsible for its interaction with membranes.
• Stathmin 3 (SCG10-like protein; SCLIP) [ 4 ]; a protein specifically expressed in neurons.
• Stathmin 4 (Stathmin-like protein B3); which contains an additional N- terminal hydrophobic domain [ 5 ].

These proteins possess a stathmin-like domain (SLD) with various N-terminal extensions. SLD is a highly conserved domain of 149 amino acid residues. Structurally, it consists of an N-terminal domain of about 45 residues followed by a 78 residue alpha-helical domain consisting of a heptad repeat coiled coil structure and a C-terminal domain of 25 residues [ 6 , 7 ]. The SLD binds two tubulins arranged longitudinally, head-to-tail, in protofilament-like complexes.

1. Stathmin: a relay phosphoprotein for multiple signal transduction? Trends Biochem. Sci. 16, 301-5
2. Role of the microtubule destabilizing proteins SCG10 and stathmin in neuronal growth. J. Neurobiol. 58, 60-9
3. The catastrophe-promoting activity of ectopic Op18/stathmin is required for disruption of mitotic spindles but not interphase microtubules. Mol. Biol. Cell 12, 73-83
4. SCLIP: a novel SCG10-like protein of the stathmin family expressed in the nervous system. J. Neurochem. 70, 2386-96
5. The stathmin family -- molecular and biological characterization of novel mammalian proteins expressed in the nervous system. Eur. J. Biochem. 248, 794-806
6. Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain. Nature 428, 198-202
7. Stathmin family proteins display specific molecular and tubulin binding properties. J. Biol. Chem. 276, 16146-54