BAIT

TUB2

ARM10, SHE8, beta-tubulin, L000002388, YFL037W
Beta-tubulin; associates with alpha-tubulin (Tub1p and Tub3p) to form tubulin dimer, which polymerizes to form microtubules; mutation in human ortholog is associated with congenital fibrosis of the extraocular muscles (CFEOM) with polymicrogyria
Saccharomyces cerevisiae (S288c)
PREY

STU2

L000003019, YLR045C
Microtubule-associated protein (MAP) of the XMAP215/Dis1 family; regulates microtubule dynamics during spindle orientation and metaphase chromosome alignment; interacts with spindle pole body component Spc72p
GO Process (2)
GO Function (2)
GO Component (5)
Saccharomyces cerevisiae (S288c)

Co-crystal Structure

Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

Publication

A TOG:αβ-tubulin complex structure reveals conformation-based mechanisms for a microtubule polymerase.

Ayaz P, Ye X, Huddleston P, Brautigam CA, Rice LM

Stu2p/XMAP215/Dis1 family proteins are evolutionarily conserved regulatory factors that use αβ-tubulin-interacting tumor overexpressed gene (TOG) domains to catalyze fast microtubule growth. Catalysis requires that these polymerases discriminate between unpolymerized and polymerized forms of αβ-tubulin, but the mechanism by which they do so has remained unclear. Here, we report the structure of the TOG1 domain from Stu2p bound to yeast αβ-tubulin. ... [more]

Science Aug. 17, 2012; 337(6096);857-60 [Pubmed: 22904013]

Throughput

  • Low Throughput

Additional Notes

  • structure determined for Stu2p TOG1 domain bound to alpha-beta tubulin

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
STU2 TUB2
Co-crystal Structure
Co-crystal Structure

Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

Low-BioGRID
1522172
TUB2 STU2
Negative Genetic
Negative Genetic

Mutations/deletions in separate genes, each of which alone causes a minimal phenotype, but when combined in the same cell results in a more severe fitness defect or lethality under a given condition. This term is reserved for high or low throughput studies with scores.

High-0.7414BioGRID
1931236
STU2 TUB2
Reconstituted Complex
Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Low-BioGRID
-
TUB2 STU2
Synthetic Rescue
Synthetic Rescue

A genetic interaction is inferred when mutations or deletions of one gene rescues the lethality or growth defect of a strain mutated or deleted for another gene.

Low-BioGRID
160319
TUB2 STU2
Two-hybrid
Two-hybrid

Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.

Low-BioGRID
-

Curated By

  • BioGRID