ArticleThe Journal of cell biology2015
Kar1 binding to Sfi1 C-terminal regions anchors the SPB bridge to the nuclear envelope.
Article in The Journal of cell biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 24 citations in OpenAlex.
- Ultrastructure expansion microscopy reveals the cellular architecture of budding and fission yeast.Journal of cell science · 2022Article
- A role for Rad5 in ribonucleoside monophosphate (rNMP) tolerance.Life science alliance · 2021Article
- The N-terminus of Sfi1 and yeast centrin Cdc31 provide the assembly site for a new spindle pole body.The Journal of cell biology · 2021Article
- Article
- Key phosphorylation events in Spc29 and Spc42 guide multiple steps of yeast centrosome duplication.Molecular biology of the cell · 2018Article
- The half-bridge component Kar1 promotes centrosome separation and duplication during budding yeast meiosis.Molecular biology of the cell · 2018Article
- Review
- Characterization of spindle pole body duplication reveals a regulatory role for nuclear pore complexes.The Journal of cell biology · 2017Article
- Molecular model of fission yeast centrosome assembly determined by superresolution imaging.The Journal of cell biology · 2017Article
- Cleavage of the SUN-domain protein Mps3 at its N-terminus regulates centrosome disjunction in budding yeast meiosis.PLoS genetics · 2017Article
- Duplication of the Yeast Spindle Pole Body Once per Cell Cycle.Molecular and cellular biology · 2016Review
- Article
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The yeast spindle pole body (SPB) is the functional equivalent of the mammalian centrosome. The half bridge is a SPB substructure on the nuclear envelope (NE), playing a key role in SPB duplication. Its cytoplasmic components are the membrane-anchored Kar1, the yeast centrin Cdc31, and the Cdc31-binding protein Sfi1. In G1, the half bridge expands into the bridge through Sfi1 C-terminal (Sfi1-CT) dimerization, the licensing step for SPB duplication. We exploited photo-activated localization microscopy (PALM) to show that Kar1 localizes in the bridge center. Binding assays revealed direct interaction between Kar1 and C-terminal Sfi1 fragments. kar1Δ cells whose viability was maintained by the dominant CDC31-16 showed an arched bridge, indicating Kar1's function in tethering Sfi1 to the NE. Cdc31-16 enhanced Cdc31-Cdc31 interactions between Sfi1-Cdc31 layers, as suggested by binding free energy calculations. In our model, Kar1 binding is restricted to Sfi1-CT and Sfi1 C-terminal centrin-binding repeats, and centrin and Kar1 provide cross-links, while Sfi1-CT stabilizes the bridge and ensures timely SPB separation.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.