An E3-like Factor that Promotes SUMO Conjugation to the Yeast Septins

Johnson, Erica S.; Gupta, Aseem A.

doi:10.1016/s0092-8674(01)00491-3

Cited by 577 publications

(583 citation statements)

References 40 publications

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“…Preventing SUMO attachment to septins Cdc3 and Cdc11 by mutagenesis of the relevant Lys residues to Ala causes 'old' septin rings to persist. By contrast, preventing SUMO attachment to the same septins by inactivation of the major SUMO ligase (by a siz1Δ mutation) does not cause the same phenotype [63]. These newer findings cast doubt on the suggestion that SUMOylation is required for disassembly of septin rings after completion of cytokinesis.…”

Section: Phosphorylation Exerts Temporal Control On Septin-collar Assmentioning

confidence: 98%

Some assembly required: yeast septins provide the instruction manual

Versele

Thorner

2005

Trends in Cell Biology

195

194

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Septins are a family of conserved proteins that form hetero-oligomeric complexes that assemble into filaments. The filaments can be organized into linear arrays, coils, rings and gauzes. They serve as membrane-associated scaffolds and as barriers to demarcate local compartments, especially for the establishment of the septation site for cytokinesis. Studies in budding and fission yeast have revealed many of the protein-protein interactions that govern the formation of multi-septin complexes. GTP binding and phosphorylation direct the polymerization of filaments that is required for septin-collar assembly in budding yeast, whereas a homolog of anillin instructs timely formation of the ring of septin filaments at the medial cortex in fission yeast. These insights should aid understanding of the organization and function of the diverse septin structures in animal cells.

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Section: Phosphorylation Exerts Temporal Control On Septin-collar Assmentioning

confidence: 98%

Some assembly required: yeast septins provide the instruction manual

Versele

Thorner

2005

Trends in Cell Biology

195

194

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“…This defect was further exacerbated in siz1 siz2 slx5 or siz1 siz2 slx8 triple mutants (Table 2). On their own, siz1 siz2 double mutants displayed a synthetic growth defect [10,42] with a doubling time (DT) of 123 min, and loss of SLX5 or SLX8Δ in this background exacerbated this defect (DT = 200 min). The fact that all of these proteins contain RING-or SP-RING motifs suggested that Siz1 and/or Siz2 may functionally overlap with, or regulate the levels of Slx5 and Slx8.…”

Section: Genetic Interactions Between Slx5-8 and Components Of The Sumentioning

confidence: 99%

“…The homologous Siz1/Ull1 and Siz2/Nfi1 proteins were the first SUMO E3 ligases to be identified [10]. These proteins share a RINGfinger related sequence motif, the SP-RING domain, with the PIAS1 (Protein Inhibitor of Activated Signal transducer and activator of transcription) protein of human cells [11,12].…”

Section: Introductionmentioning

confidence: 99%

“…These proteins share a RINGfinger related sequence motif, the SP-RING domain, with the PIAS1 (Protein Inhibitor of Activated Signal transducer and activator of transcription) protein of human cells [11,12]. The Siz1 and Siz2 ligases are active on septins and may have partially overlapping specificities [10,13,14]. Together, Siz1 and Siz2 account for 90% of the total sumoylation in yeast, and cells lacking both SIZ1 and SIZ2 are viable but slow growing [9,10].…”

Section: Introductionmentioning

confidence: 99%

“…The Siz1 and Siz2 ligases are active on septins and may have partially overlapping specificities [10,13,14]. Together, Siz1 and Siz2 account for 90% of the total sumoylation in yeast, and cells lacking both SIZ1 and SIZ2 are viable but slow growing [9,10]. The SIZ-independent sumoylation may be partly due to a third ligase, Mms21, which is essential for viability and also contains an SP-RING domain [15,16].…”

Section: Introductionmentioning

confidence: 99%

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Stimulation of in vitro sumoylation by Slx5–Slx8: Evidence for a functional interaction with the SUMO pathway

et al. 2007

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The yeast genes SLX5 and SLX8 were identified based on their requirement for viability in the absence of the Sgs1 DNA helicase. Loss of these genes results in genome instability, nibbled colonies, and other phenotypes associated with defects in sumoylation. The Slx5 and Slx8 proteins form a stable complex and each subunit contains a single RING-finger domain at its C-terminus. To determine the physiological function of the Slx5-8 complex, we explored its interaction with the SUMO pathway. Curing 2μ circle from the mutants suppressed their nibbled colony phenotype and partially improved their growth rate, but did not affect their sensitivity to hydroxyurea. The increase in sumoylation observed in slx5Δ and slx8Δ mutants was found to be dependent on the Siz1 SUMO ligase. Physical interactions between the Slx5-8 complex and both Ubc9 and Smt3 were identified and characterized. Using in vitro reactions, we show that Slx5, Slx8, or the Slx5-8 complex stimulates the formation of SUMO chains and the sumoylation of a test substrate. Interestingly, a functional RING-finger domain is not required for this stimulation in vitro. These biochemical data demonstrate for the first time that the Slx5-8 complex is capable of interacting directly with the SUMO pathway.

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Studies of the Ubiquitin Proteasome System

et al. 2006

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A concept that has arisen over the last decade is that proteins can, in general, be covalently modified by polypeptides, resulting in alterations in their fate and function. The first‐identified and most well studied of these modifying polypeptides is ubiquitin. Although targeting for proteasomal degradation is the best studied outcome of ubiquitylation, we now understand that modification of proteins with ubiquitin has numerous other cellular roles that alter protein function and that are unrelated to proteasomal degradation. Ubiquitylation is a complex process that is regulated at the level of both addition and removal of ubiquitin from target proteins. This unit includes a number of different basic protocols that will facilitate the study of components of the ubiquitin system and substrate ubiquitylation both in vitro and in cells. Because another protein modifier, NEDD8, itself regulates aspects of the ubiquitin system, basic protocols on neddylation are also included in this unit.

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An E3-like Factor that Promotes SUMO Conjugation to the Yeast Septins

Cited by 577 publications

References 40 publications

Some assembly required: yeast septins provide the instruction manual

Some assembly required: yeast septins provide the instruction manual

Stimulation of in vitro sumoylation by Slx5–Slx8: Evidence for a functional interaction with the SUMO pathway

Studies of the Ubiquitin Proteasome System

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