The yeast homologue of the microtubule-associated protein Lis1 interacts with the sumoylation machinery and a SUMO-targeted ubiquitin ligase

Alonso, Annabel; D’Silva, Sonia; Rahman, Maliha; Meluh, Pam B.; Keeling, Jacob; Meednu, Nida; Hoops, Harold J.; Miller, Rita K.

doi:10.1091/mbc.e12-03-0195

Cited by 17 publications

(40 citation statements)

References 95 publications

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“…Stu2p also interacts with several other microtubule‐associated proteins, including the spindle positioning protein Kar9p, the CLIP‐170 homologue Bik1p, the EB1 homolog Bim1p, and the kinetochore protein Ndc80p (Alonso et al, ; Blake‐Hodek, Cassimeris, & Huffaker, ; Miller, Cheng, & Rose, ; Wolyniak et al, ; Wong et al, ). Each of these interacts with SUMO (Alonso et al, ; Leisner et al, ; Meednu et al, ; Montpetit, Hazbun, Fields, & Hieter, ). Therefore, we tested whether STU2 might also interact with SUMO using a two‐hybrid assay.…”

Section: Resultsmentioning

confidence: 99%

“…This finding suggests that the Stu2p‐Pac1p interaction does not require the TOG domains of Stu2p. As Pac1p/Lis1 was recently demonstrated to be sumoylated, this represents the fifth sumoylated MAP with which Stu2p interacts (Alonso et al, ; Meednu et al, ; Montpetit et al, ).…”

Section: Resultsmentioning

confidence: 99%

“…We next examined the possibility that SUMO could be attached to Stu2p using an in vitro sumoylation assay, described previously (Alonso et al, ; Meednu et al, ). For this, a Stu2‐TAP tag fusion was purified from yeast and components of the sumoylation pathway including SUMO, Ubc9p and Aos1/Uba2p were purified from bacteria (Puig et al, ).…”

Section: Resultsmentioning

confidence: 99%

“…We have previously posited a model for the regulation of the MAP Pac1p/Lis1 by STUbLs and the proteasome (Alonso et al, ). Consistent with this model, we show that Stu2p also interacts with the STUbL enzyme Ris1p and ubiquitin.…”

Section: Discussionmentioning

confidence: 99%

“…With this work on Stu2p, eight different classes of MAPs have now been shown to interact with SUMO. These are tau (Dorval and Fraser, ), Ndc80p (Montpetit et al, ), CENP‐E (Zhang et al, ), Kar9p and Bim1p/EB1 (Leisner et al, ; Meednu et al, ), as well as Pac1p/Lis1 and Bik1p/CLIP‐170 (Alonso et al, ). Interestingly, Stu2p interacts with five of these.…”

Section: Discussionmentioning

confidence: 99%

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The TOG protein Stu2/XMAP215 interacts covalently and noncovalently with SUMO

et al. 2018

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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.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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The TOG protein Stu2/XMAP215 interacts covalently and noncovalently with SUMO

et al. 2018

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SUMO ylation

Kerscher

2016

Encyclopedia of Life Sciences

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Eukaryotic cells utilise the dynamic addition and removal of SUMO, a small ubiquitin‐like modifier (UBL), to modulate protein functions, interactions and localisation. Protein SUMOylation involves a cascade of dedicated enzymes that facilitate the covalent modification of specific lysine residues on target proteins with monomers or polymers of SUMO. The cellular homeostasis of SUMOylated proteins is also regulated by SUMO proteases and SUMO‐targeted ubiquitin ligase (STUbLs). SUMO proteases cleave SUMO from modified proteins. In contrast, STUbLs ubiquitinate proteins modified with SUMO chains. Recent data suggests that ubiquitination via STUbLs effects the turnover of SUMOylated proteins as well as the spatio‐temporal composition of complexes that contain SUMO‐modified proteins. Defects in the controlled addition, removal and turnover of SUMO‐modified proteins greatly affect cellular fitness and contribute to developmental defects, cancer and protein aggregation disorders. Key Concepts SUMO encodes a small ubiquitin‐like modifier that is covalently attached to lysines in target proteins. SUMOylation, the process of SUMO conjugation to a target protein, frequently occurs on a lysine situated in a SUMOylation consensus site. SUMO conjugates can be removed from target proteins by SUMO‐specific proteases. Vertebrates express three different SUMO isoforms: SUMO1, SUMO2 and SUMO3, encoded by three different genes. SUMOs can form polymers via internal SUMOylation sites in SUMO2 and SUMO3. Several proteins can bind non‐covalently to SUMOs via SUMO interaction motifs (SIMs). A finely balanced SUMOylation/de‐SUMOylation system is required for eukaryotic life. Cross‐talk between SUMOylation and ubiquitination plays a critical in the turnover of some SUMOylated proteins as well as the spatiotemporal composition of complexes that contain SUMO‐modified proteins.

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Stopped in its tracks: Negative regulation of the dynein motor by the yeast protein She1

Moore

2013

BioEssays

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Summary How do cells direct the microtubule motor protein dynein to move cellular components to the right place at the right time? Recent studies in budding yeast shed light on a new mechanism for directing dynein, involving the protein She1. She1 restricts where and when dynein moves the nucleus and mitotic spindle. Experiments with purified proteins show that She1 binds to microtubules and inhibits dynein by stalling the motor on its track. Here I describe what we have learned so far about She1, based on a combination of genetic, cell biology, and biophysical approaches. These findings set the stage for further interrogation of the She1 mechanism, and raise the question of whether similar mechanisms exist in other species.

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The yeast homologue of the microtubule-associated protein Lis1 interacts with the sumoylation machinery and a SUMO-targeted ubiquitin ligase

Cited by 17 publications

References 95 publications

The TOG protein Stu2/XMAP215 interacts covalently and noncovalently with SUMO

The TOG protein Stu2/XMAP215 interacts covalently and noncovalently with SUMO

SUMO ylation

Stopped in its tracks: Negative regulation of the dynein motor by the yeast protein She1

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