The TOG protein Stu2/XMAP215 interacts covalently and noncovalently with SUMO
| Autor: | Nida Meednu, Kayla J. Davis, Annabel Alonso, Victoria Tabb, Maliha Rahman, Rita K. Miller, River Cook, Matt Greenlee |
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| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Saccharomyces cerevisiae Proteins Ubiquitin-Protein Ligases genetic processes Saccharomyces cerevisiae SUMO protein macromolecular substances Microtubules environment and public health Microtubule polymerization 03 medical and health sciences Ubiquitin Structural Biology Microtubule ubiquitin XMAP215 Research Articles STU2 chemistry.chemical_classification biology Sumoylation Cell Biology biology.organism_classification Yeast Cell biology enzymes and coenzymes (carbohydrates) 030104 developmental biology Enzyme Tubulin tubulin chemistry SUMO health occupations biology.protein Microtubule-Associated Proteins Research Article |
| Zdroj: | Cytoskeleton (Hoboken, N.j.) |
| ISSN: | 1949-3592 1949-3584 |
| DOI: | 10.1002/cm.21449 |
| Popis: | Stu2p is the yeast member of the XMAP215/Dis1/ch‐TOG family of microtubule‐associated proteins that promote microtubule polymerization. However, the factors that regulate its activity are not clearly understood. Here we report that Stu2p in the budding yeast Saccharomyces cerevisiae interacts with SUMO by covalent and noncovalent mechanisms. Stu2p interacted by two‐hybrid analysis with the yeast SUMO Smt3p, its E2 Ubc9p, and the E3 Nfi1p. A region of Stu2p containing the dimerization domain was both necessary and sufficient for interaction with SUMO and Ubc9p. Stu2p was found to be sumoylated both in vitro and in vivo. Stu2p copurified with SUMO in a pull‐down assay and vice versa. Stu2p also bound to a nonconjugatable form of SUMO, suggesting that Stu2p can interact noncovalently with SUMO. In addition, Stu2p interacted with the STUbL enzyme Ris1p. Stu2p also copurified with ubiquitin in a pull‐down assay, suggesting that it can be modified by both SUMO and ubiquitin. Tubulin, a major binding partner of Stu2p, also interacted noncovalently with SUMO. By two‐hybrid analysis, the beta‐tubulin Tub2p interacted with SUMO independently of the microtubule stressor, benomyl. Together, these findings raise the possibility that the microtubule polymerization activities mediated by Stu2p are regulated through sumoylation pathways. |
| Databáze: | OpenAIRE |
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