FEATURES

FAMILY

DESCRIPTION

Also known as STU2_YEAST, STU2. Binds to the plus end of microtubules and regulates microtubule dynamics and microtubule organization. May play a role in the attachment, organization, and/or dynamics of microtubule ends at the spindle pole body. Stabilizes both cytoplasmic and nuclear microtubules. Promotes mitotic spindle elongation in anaphase. Has microtubule polymerase activity by accelerating microtubule growth and inhibiting catastrophe. The polymerase activity is proposed to involve a tethering mechanism at the microtubule plus end: a curved, longitudinally microtubule lattice-associated tubulin heterodimer (that cannot be incorporated into the microtubule lattice) is bound via one TOG domain while the other TOG domain binds to an unpolymerized tubulin heterodimer leading to lateral association of these tubulin heterodimers; polymerization-induced straightening of the tubulin heterodimer releases the polymerase (PubMed:11309422, PubMed:25172511, PubMed:16567500, PubMed:25097237). Is involved in regulation of kinetochore-microtubule attachments in a tension-dependent manner involving its association with the NDC80 complex; the function may be independent of its microtubule polymerase activity. Can either stabilize or destabilize kinetochore attachments, depending on the level of kinetochore tension and whether the microtubule tip is assembling or disassembling (PubMed:27156448). Binds to microtubules. Homodimer; each monomer can bind via its TOG domains to two alpha/beta-tubulin heterodimers. Interacts with SPC72. Associates with the NDC80 complex.

EXTERNAL LINKS

STU2

Mutations

Mutation(s) distribution

Mutations table