The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
The Spc105/Kre28 complex promotes mitotic error correction by outer kinetochore recruitment of Ipl1/Sli15
Open accessPreprint — published as 10.1038/s44318-025-00437-w · Paper page
Abstract
Kinetochores link chromosomes to dynamic microtubules of the mitotic spindle. To ensure equal chromosome segregation, sister chromatids must achieve biorientation. The conserved kinase Aurora B phosphorylates outer kinetochore proteins on attachments lacking tension, allowing re-establishment of new connections until biorientation is achieved. Aurora B localizes to the centromere as part of the chromosomal passenger complex (CPC), but the underlying recruitment pathways can be eliminated without disrupting biorientation. It therefore remains unclear how the kinase operates during error correction. Here, we identify the conserved Spc105/Kre28 complex as an outer kinetochore receptor of the Aurora kinase Ipl1 and its activator Sli15 in Saccharomyces cerevisiae . We show that mutations in the helix bundle domain of Spc105/Kre28 impair mitotic error correction, resembling the effects of ipl1 or sli15 mutants. The defects can be suppressed by artificial recruitment of Ipl1. In biochemical experiments Ipl1/Sli15 directly associates with Spc105/Kre28, and a conserved segment in the Sli15 central domain is crucially involved in the binding mechanism. These results have important implications for the mechanism of tension-dependent error correction during chromosome biorientation.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
Flagged first, then by citations
Research works printed but not linked: 65
- 10.1038/S41586-024-07487-W · DOI · Paper page
- 10.1038/nature09594 · DOI
- 10.1101/gad.934801 · DOI
- 10.1083/jcb.201905144 · DOI
- 10.1083/jcb.201306054 · DOI
- 10.1038/nature12057 · DOI
- 10.1016/j.cell.2008.03.020 · DOI
- 10.1038/s41467-022-29542-8 · DOI
- 10.1126/sciadv.adg7480 · DOI · Paper page
- 10.1101/gad.1126303 · DOI
- 10.1016/j.cell.2016.10.011 · DOI
- 10.1093/nar/gkv332 · DOI
- Evans R , O’Neill M , Pritzel A , Antropova N , Senior A , Green T , Žídek A , Bates R , Blackwell S , Yim J , et al (2022) Protein complex prediction with AlphaFold-Multimer. bioRxiv: 2021.2010.2004.463034 · DOI · Paper page
- 10.15252/msb.202211084 · DOI
- 10.7554/eLife.42879 · DOI
- 10.1016/j.cub.2019.03.051 · DOI
- 10.1016/j.cell.2008.09.046 · DOI
- 10.1016/j.celrep.2020.108190 · DOI
- 10.1083/jcb.201907087 · DOI
- 10.1126/science.1221483 · DOI
- 10.3389/fcell.2017.00112 · DOI
- 10.1083/jcb.201403081 · DOI
- 10.1126/science.1101366 · DOI
- 10.1016/j.cell.2007.07.045 · DOI
- 10.1126/science.1235532 · DOI
- 10.1093/bib/bbx108 · DOI · Paper page
- 10.3389/fonc.2015.00225 · DOI
- 10.1016/j.jmb.2007.05.022 · DOI
- 10.1002/1097-0061(20000630)16:9<857::AID-YEA561>3.0.CO;2-B · DOI
- 10.1016/j.cub.2023.09.006 · DOI
- 10.1126/science.1167000 · DOI
- 10.1016/j.cub.2012.03.052 · DOI
- 10.1038/emboj.2012.356 · DOI
- 10.1016/j.devcel.2011.05.008 · DOI
- 10.1038/S41592-022-01488-1 · DOI · Paper page
- 2017, A Molecular View of Kinetochore Assembly and Function, Biology (Basel), 6, 5
- 10.1038/ncb3065 · DOI
- 10.1371/journal.pone.0007640 · DOI
- 10.1016/j.cub.2024.04.054 · DOI
- 10.1093/NAR/GKAB1038 · DOI · Paper page
- 10.1016/j.molcel.2022.04.027 · DOI
- 10.1016/j.cell.2016.10.005 · DOI
- 10.1016/j.molcel.2014.01.019 · DOI
- 10.1002/jcc.20084 · DOI
- 10.1016/j.cub.2024.03.062 · DOI · Paper page
- 10.1038/s41594-024-01230-9 · DOI
- 10.1016/j.cub.2011.04.011 · DOI
- 10.1098/rsob.210274 · DOI
- 10.1038/embor.2012.1 · DOI
- 10.1016/j.molcel.2005.03.031 · DOI
- 10.1016/j.cub.2012.03.051 · DOI
- 10.1016/j.cub.2018.08.038 · DOI
- 10.3390/cells11091462 · DOI
- 10.1073/pnas.1821945116 · DOI
- 10.1038/nmeth.2103 · DOI
- 10.1016/j.cell.2009.03.035 · DOI
- 10.1093/bioinformatics/btp033 · DOI
- 10.1038/nsmb1186 · DOI
- 10.1038/nature19333 · DOI
- 10.1083/jcb.200804170 · DOI
- 10.1101/gad.304782.117 · DOI
- 10.1038/ncb2515 · DOI
- 10.1126/SCIENCE.ABN3810/SUPPL_FILE/SCIENCE.ABN3810_MOVIES_S1_AND_S2.ZIP · DOI
- 10.1038/s41594-024-01249-y · DOI · Paper page
- 10.1016/j.cub.2024.04.067 · DOI
Metadata
- Authors
- Dudziak, A., Pleuger, R., Schmidt, J., Hamm, F., Tendulkar, S., Jänen, K., Vetter, I. R., Singh, S., Fischböck, J., Herzog, F., & Westermann, S.
- Affiliations
- University of Duisburg-Essen (DE)
- Max Planck Institute of Molecular Physiology (DE)
- Ludwig-Maximilians-Universität München (DE)
- IMC University of Applied Sciences Krems (AT)
- Corresponding author
- Westermann, Stefan
- ORCID
- Venue
- The EMBO Journal
- Publisher
- openRxiv
- Published
- 2024-10-02
- Volume
- 44
- Issue
- 12
- Pages
- 3492-3520
- ISSN
- 0261-4189 (ISSN-L)
- PMC
- PMC12170873
- OpenAlex
- W4409781585
- Cited by
- 4
- References
- 1
- Citations by year
- 2026: 4
- FWCI
- 2.00
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- The EMBO Journal (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Universitätsbibliographie, Universität Duisburg-Essen (submittedVersion)
- DuEPublico (University of Duisburg-Essen) (submittedVersion, cc-by)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Funders
- Deutsche Forschungsgemeinschaft (424228829)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Keywords
- Aurora B kinase, outer kinetochore, chromosome biorientation, chromosomal passenger complex, kinetochore-microtubule attachment, protein-protein interaction, Saccharomyces cerevisiae
- MeSH terms
- Microtubule-Associated Proteins, Mitosis, Mutation, Saccharomyces cerevisiae, Protein Serine-Threonine Kinases, Kinetochores, Cell Cycle Proteins, Chromosome Segregation, Saccharomyces cerevisiae Proteins, Intracellular Signaling Peptides and Proteins, Aurora Kinases
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review