The TOG protein Stu2/XMAP215 interacts covalently and noncovalently with SUMO
Author:
Affiliation:
1. Department of Biochemistry and Molecular BiologyOklahoma State UniversityStillwater Oklahoma74078
2. Department of BiologyUniversity of RochesterRochester New York14627
Funder
Oklahoma Center for the Advancement of Science and Technology
NSF
NIH
Oklahoma Agricultural Experiment Station
Publisher
Wiley
Subject
Cell Biology,Structural Biology
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1002/cm.21449
Reference84 articles.
1. Protection from Free β-Tubulin by the β-Tubulin Binding Protein Rbl2p
2. Regulation of microtubule dynamics by TOG-domain proteins XMAP215/Dis1 and CLASP
3. Crystal Structure of a TOG Domain: Conserved Features of XMAP215/Dis1-Family TOG Domains and Implications for Tubulin Binding
4. Stu2p binds tubulin and undergoes an open-to-closed conformational change
5. The yeast homologue of the microtubule-associated protein Lis1 interacts with the sumoylation machinery and a SUMO-targeted ubiquitin ligase
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1. Aspergillus SUMOylation mutants exhibit chromosome segregation defects including chromatin bridges;GENETICS;2023-09-19
2. Robust microtubule dynamics facilitate low-tension kinetochore detachment in metaphase;Journal of Cell Biology;2023-05-11
3. Aspergillus SUMOylation mutants have normal dynein function but exhibit chromatin bridges;2023-04-18
4. The TOG protein Stu2 is regulated by acetylation;PLOS Genetics;2022-09-09
5. The TOG protein Stu2 is regulated by acetylation;2022-01-02
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