Mutational analysis of op18/stathmin-tubulin-interacting surfaces. Binding cooperativity controls tubulin GTP hydrolysis in the ternary complex.

@article{Segerman2000MutationalAO,
  title={Mutational analysis of op18/stathmin-tubulin-interacting surfaces. Binding cooperativity controls tubulin GTP hydrolysis in the ternary complex.},
  author={Bo Segerman and Niklas Larsson and Per Holmfeldt and Martin Gullberg},
  journal={The Journal of biological chemistry},
  year={2000},
  volume={275 46},
  pages={35759-66}
}
Oncoprotein 18 (Op18) is a microtubule regulator that forms a ternary complex with two tubulin heterodimers. Dispersed regions of Op18 are involved in two-site cooperative binding and subsequent modulation of tubulin GTPase activity. Here we have analyzed specific determinants of Op18 that govern both stoichiometry and positive cooperativity in tubulin binding and consequent stimulatory and inhibitory effects on tubulin GTPase activity. The data revealed that the central and C-terminal regions… CONTINUE READING