| 2006 |
Human SGO1 directly binds to protein phosphatase 2A (PP2A). PP2A localizes to centromeres in a Bub1-dependent manner, and the SGO1-PP2A interaction is required for centromeric localization of SGO1. Depletion of Plk1 by RNAi restores centromeric SGO1 localization in PP2A-depleted cells, indicating that Bub1 targets PP2A to centromeres which counteracts Plk1-mediated removal of SGO1. |
Co-immunoprecipitation, RNAi depletion, immunofluorescence localization, epistasis analysis |
Developmental cell |
High |
16580887
|
| 2012 |
CDK-mediated mitosis-specific phosphorylation of SGO1 activates its cohesion-protection function and enables direct binding of SGO1 to cohesin. The phospho-SGO1-bound cohesin complex contains PP2A, PDS5, and hypophosphorylated sororin, but lacks WAPL. SGO1-PP2A dephosphorylates PDS5-bound sororin, protecting centromeric cohesin from WAPL. Expression of non-phosphorylatable sororin bypasses the requirement for SGO1-PP2A in centromeric cohesion. |
In vitro kinase assay, co-immunoprecipitation, RNAi, phospho-mutant expression, rescue experiments |
Nature cell biology |
High |
23242214
|
| 2015 |
SGO1 is a direct reader of the Bub1-mediated histone H2A-pT120 mark. Bub1 recruits RNA Polymerase II (Pol II) to unattached kinetochores, promoting mitotic transcription. Mitosis-specific inactivation of Pol II traps SGO1 at kinetochores and weakens centromeric cohesion. SGO1 interacts with Pol II in human cells and with RNA in vitro, suggesting Pol II-dependent transcription enables kinetochore-bound SGO1 to reach cohesin embedded in centromeric chromatin. |
Co-immunoprecipitation, RNA-binding assay in vitro, Pol II inactivation, immunofluorescence, ChIP |
Molecular cell |
High |
26190260
|
| 2013 |
Cohesin and histone H2A-pT120 specify two distinct pools of SGO1-PP2A: one at inner centromeres (cohesin-bound) and one at kinetochores (H2A-pT120-bound). Bub1 inactivation delocalizes cohesin-SGO1 to chromosome arms. Kinetochore tension triggers SGO1 dephosphorylation and redistributes SGO1 from inner centromeres to kinetochores; incomplete redistribution causes chromosome nondisjunction. |
RNAi, phospho-mutant expression, immunofluorescence, tension perturbation experiments |
Current biology : CB |
High |
24055156
|
| 2005 |
Budding yeast Sgo1 is required for sensing lack of tension at the kinetochore in mitosis. SGO1 mutant cells respond normally to microtubule depolymerization but fail to respond to lack of tension, and have difficulty attaching sister chromatids to opposite poles (biorientation defect). Degradation of Sgo1 when sister chromatids separate prevents cell cycle arrest in anaphase. |
Genetic mutant analysis, spindle checkpoint assays, chromosome segregation assays in S. cerevisiae |
Science (New York, N.Y.) |
High |
15637284
|
| 2009 |
In Xenopus egg extract reconstitution, Sgo1 plays a role in stabilizing cohesin along chromosome arms during prophase. This stabilizing activity is antagonized by the mitotic kinases Plk1 and Aurora B, which promotes sister chromatid resolution. |
Xenopus egg extract in vitro reconstitution, immunodepletion, functional rescue |
Genes & development |
High |
19696148
|
| 2008 |
The short splice variant of SGO1 (sSgo1) localizes to the centrosome in interphase and to spindle poles in mitosis. sSgo1 interacts with Plk1, and its spindle pole localization is Plk1-dependent. sSgo1 is required for centriole cohesion; its depletion causes separation of paired centrioles, and this can be suppressed by sSgo1 re-expression or Plk1 knockdown. |
GFP localization, co-immunoprecipitation, RNAi, dominant-negative mutant expression, centrosome imaging |
Developmental cell |
High |
18331714
|
| 2007 |
NEK2A directly binds human SGO1 in vitro and co-localizes with SGO1 at kinetochores. NEK2A phosphorylates SGO1 at Ser14 and Ser507. Non-phosphorylatable SGO1 mutants perturb chromosome congression and cause increased microtubule attachment errors (syntelic and monotelic attachments), though phosphorylation is not required for SGO1 assembly at kinetochores. |
In vitro pulldown, in vitro phosphorylation assay with 32P incorporation, phospho-site mapping, expression of phospho-mutants, immunofluorescence |
Cell research |
High |
17621308
|
| 2014 |
In budding yeast, Sgo1 together with PP2A-Rts1 ensures localization of condensin to centromeric chromatin. Sgo1 is also required for maintaining Aurora B/Ipl1 localization on kinetochores during metaphase. Thus Sgo1 has a dual function in promoting chromosome biorientation: modulating pericentric chromatin conformation via condensin, and maintaining Aurora B/Ipl1 at kinetochores. |
Genetic epistasis, chromatin immunoprecipitation (ChIP), immunofluorescence, yeast genetics |
PLoS genetics |
Medium |
24945276
|
| 2008 |
Human SGO1 is degraded during mitotic exit and is a substrate of APC/C-Cdh1. SGO1 contains both a KEN box and a D-box; deletion of either motif alone is insufficient to stabilize SGO1, but simultaneous deletion of both renders it stable. Non-degradable SGO1 does not impair mitotic progression or sister-chromatid separation, indicating SGO1 degradation is not required for these processes. Bub1 contributes to SGO1 steady-state levels via an APC/C-independent mechanism. |
Ubiquitination assay in vitro, overexpression/knockdown, deletion mutagenesis, cell cycle synchronization, western blot |
The Journal of biological chemistry |
High |
19015261
|
| 2005 |
In budding yeast, Sgo1 localizes to cohesin-associated regions (CARs) at the centromere and a 50-kb pericentric domain during meiosis I. Establishment of this domain requires the 120-bp core centromere, Bub1, and the meiosis-specific factor Spo13. Cohesins and kinetochore proteins Iml3/Chl4 are necessary for Sgo1 to associate with pericentric but not core centromeric regions. This 50-kb Sgo1-binding domain is where cohesins are protected from removal during meiosis I. |
ChIP, genetic epistasis, localization studies in S. cerevisiae meiosis |
Genes & development |
High |
16357219
|
| 2010 |
SGO1 is first recruited to centromeric heterochromatin in G2 in an HP1-dependent manner that does not require Bub1 kinase activity. In prophase, SGO1 becomes diffusely localized, then returns to centromeres in a Bub1 kinase-dependent manner. Despite the absence of SGO1 from mitotic centromeres when Bub1 kinase is absent, centromeric cohesion is maintained, suggesting the G2 recruitment establishes the initial protection mechanism. |
BUB1-null MEF complementation assay, immunofluorescence, kinase-dead Bub1 expression, cell cycle staging |
Journal of cell science |
Medium |
20124418
|
| 2011 |
HP1α is targeted to mitotic centromeres by INCENP (a CPC subunit), not by SGO1. Both HP1-INCENP and HP1-SGO1 interactions require the HP1 chromo shadow domain binding to PXVXL/I motifs. An SGO1 mutant deficient in HP1 binding is fully functional in centromeric cohesion protection and localizes normally to centromeres in mitosis. HP1 binding by SGO1 is required for interphase centromere localization but dispensable for mitotic cohesion protection. |
Biochemical and structural analysis, mutagenesis, complementation assay, immunofluorescence in human cells |
Molecular biology of the cell |
High |
21346195
|
| 2011 |
In budding yeast, overexpression of SGO1 partially corrects chromosome segregation defects of bub1Δ cells and restores viability to bub1Δ tetraploid cells. Overexpression of CPC subunits Bir1 (survivin) and Sli15 (INCENP) suppresses growth defects of both bub1Δ and sgo1Δ tetraploids. Sgo1 is identified as a possible partner of Mps1; Mps1 is required for Sgo1 kinetochore localization, and Sgo1 overexpression rescues Mps1 inactivation defects. The Bub1-Sgo1-Mps1 pathway acts independently of Aurora B for biorientation. |
High-copy suppressor screen, genetic epistasis, yeast genetics, overexpression rescue experiments |
Molecular biology of the cell |
Medium |
21389114
|
| 2014 |
In budding yeast, Sgo1 recruits the PP2A isoform containing Rts1 to the pericentromeric region prior to biorientation. Artificial recruitment of Rts1 to a single chromosome is sufficient to perform the function of Sgo1 on that chromosome, establishing that a major function of Sgo1 is to recruit PP2A-Rts1. Sgo1 is also an APC/C substrate in yeast, with mitotic destruction depending on a D-box-related motif; however, removal from chromosomes before anaphase depends on tension-responsive mechanisms rather than degradation. |
Yeast genetics, artificial centromere targeting, epistasis, cell cycle analysis |
Journal of cell science |
High |
25236599
|
| 2014 |
Aurora B kinase interacts with and phosphorylates SGO1 in vitro and in vivo. Aurora B-mediated phosphorylation regulates the distribution of SGO1 between centromeres and chromosome arms. Expression of Aurora B kinase-dead mutant forms of SGO1 causes mislocalization from centromeres to chromosome arms. |
Co-immunoprecipitation, in vitro kinase assay, phospho-mutant expression, immunofluorescence |
Biochemical and biophysical research communications |
Medium |
25451264
|
| 2022 |
Using an integrative structure-function approach, the 'histone H3-like' SGO1 N-terminal tail interaction with the Survivin BIR domain was identified as the hotspot essential for CPC-SGO1 assembly, with downstream SGO1 residues and Borealin contributing to high-affinity binding. Disrupting the SGO1-Survivin interaction abolishes CPC-SGO1 assembly and perturbs CPC centromere localization and function. SGO1 and H3T3ph use the same surface on Survivin to bind CPC. |
Structural analysis, mutagenesis, co-immunoprecipitation, functional assays in human cells |
The Journal of cell biology |
High |
35776132
|
| 2018 |
Budding yeast CENP-A (Cse4) interacts with SGO1 in vivo and in vitro. The N-terminus coiled-coil domain of Sgo1 (without the C-terminus) is sufficient for interaction with CENP-A and association with core centromeric (CEN) but not pericentric chromatin in a cell cycle-dependent manner. Depletion of CENP-A results in loss of Sgo1 from centromeric chromatin. The N-terminus is required for genome stability. |
Co-immunoprecipitation in vivo and in vitro, domain deletion analysis, ChIP, chromosome loss assay in S. cerevisiae |
Cell cycle (Georgetown, Tex.) |
Medium |
28980861
|
| 2020 |
SGO1 interacts directly with the dimerization domain of the CPC subunit Borealin in Xenopus egg extracts. Borealin and PP2A can bind simultaneously to the coiled-coil domain of SGO1. A Borealin mutant that disrupts SGO1-Borealin interaction causes defects in CPC chromosomal recruitment and Aurora B-dependent spindle assembly but not in spindle assembly checkpoint signaling at unattached kinetochores. |
Xenopus egg extract biochemical reconstitution, direct binding assay, mutagenesis, immunodepletion, functional assays |
Molecular biology of the cell |
High |
32697622
|
| 2016 |
In budding yeast, the Bub1-H2A-Sgo1-PP2A-Rts1 axis prevents premature silencing of the spindle assembly checkpoint prior to tension generation. Mutation of Bub1's kinase domain, the Bub1 phosphorylation site in H2A, or sgo1 mutants with abolished binding to H2A or PP2A-Rts1 all result in premature SAC silencing in the presence of tensionless attachment. |
Genetic epistasis, yeast mutant analysis, checkpoint assays in S. cerevisiae |
Genetics |
Medium |
28040741
|
| 2019 |
SET directly binds to a domain in SGO1 in close proximity to the cohesin-binding motif. SET disrupts SGO1-cohesin binding in a dose-dependent manner in vitro and by SET overexpression in cells. SET binding-deficient SGO1 mutant fully supports centromeric cohesion but delays chromosome segregation. SET depletion delays cohesion fatigue, and overexpression exacerbates it. Thus, SET functions during mitosis by disrupting the SGO1-cohesin interaction to promote timely chromosome segregation. |
In vitro binding assay, co-immunoprecipitation, mutagenesis, overexpression/depletion, live-cell imaging |
The Journal of cell biology |
High |
31227592
|
| 2024 |
CENP-A interacts with SGO1 and determines the localization of SGO1 to the centromere during mitosis. Lysine and arginine residues in the C-terminal domain of SGO1 are critical for CENP-A binding. Replacement of these basic residues with acidic residues perturbs localization of SGO1 and Aurora B to the centromere, resulting in aberrant chromosome segregation and premature chromatid separation. |
Co-immunoprecipitation, site-directed mutagenesis, immunofluorescence in human cells, functional chromosome segregation assay |
Journal of molecular cell biology |
Medium |
37777834
|
| 2016 |
In budding yeast, Bub1 and Sgo1 act as a rheostat to regulate pericentric chromatin structure. Histone H2A phosphorylation by Bub1 and subsequent Sgo1 recruitment softens the chromatin spring in response to changes in microtubule dynamics. In response to reduced microtubule dynamics, a Bub1/Sgo1-dependent structural change causes contraction of inner kinetochore clusters and radial expansion of pericentric chromatin, with the pericentric chromatin becoming less dynamic. |
Live-cell imaging, fluorescence imaging, genetic analysis in S. cerevisiae, quantitative chromatin dynamics measurements |
Current biology : CB |
Medium |
22365852
|
| 2006 |
Two major isoforms of human SGO1 exhibit distinct subcellular localization: the longer isoform localizes to kinetochores during G2 through mitosis, while the short isoform (sSgo1, lacking exon 6) does not localize to kinetochores but enriches at mitotic spindles and is found at S-phase foci (some colocalizing with kinetochores). These different localizations suggest isoform-specific functions during the cell cycle. |
GFP fusion localization, live-cell imaging, co-localization with CREST antigen |
Cell cycle (Georgetown, Tex.) |
Medium |
16582621
|
| 2016 |
In Xenopus cell-free system, both CENP-C and CENP-T can independently drive centromeric accumulation of SGO1 through recruitment of Bub1 to the KMN network. Mps1 is also required for this pathway. Forced targeting of Bub1 to centromeres (in the absence of other kinetochore components) is sufficient to restore SGO1 localization, demonstrating that Bub1-mediated H2A phosphorylation is the critical downstream signal. |
Xenopus egg cell-free system, immunodepletion, artificial targeting experiments, immunofluorescence |
Chromosoma |
High |
27116032
|
| 2014 |
A homozygous founder mutation in SGOL1 (K23E) causes CAID syndrome. Cultured fibroblasts from affected individuals showed accelerated cell cycle progression, higher senescence rate, and enhanced TGF-β signaling. Karyotypes showed centromeric cohesion defect (railroad appearance). Morpholino-induced knockdown of sgol1 in zebrafish recapitulated the human abnormalities including defects in enteric nervous system and smooth muscle. |
Human genetics, cell biological analysis of patient fibroblasts, zebrafish morpholino knockdown, karyotyping |
Nature genetics |
Medium |
25282101
|
| 2012 |
In budding yeast, Bub1 kinase activity is not required for spindle checkpoint function but is required for centromeric localization of Sgo1. Despite absence of centromeric Sgo1 in mitotic cells lacking Bub1 kinase activity, centromeric cohesion is still maintained until anaphase (negative result: Bub1 kinase-dependent Sgo1 centromeric localization in mitosis is not required to maintain cohesion). |
Bub1 kinase-dead MEF complementation, immunofluorescence, functional cohesion assays |
Journal of cell science (duplicate entry under PMID 20124418) |
Medium |
20124418
|