ArticleeLife2014
Cell-cycle dependent phosphorylation of yeast pericentrin regulates γ-TuSC-mediated microtubule nucleation.
Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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Who cites it
58 citing papers in PubMed, 94 citations in OpenAlex.
- The parkin-γ-tubulin axis regulates epidermal homeostasis and is associated with the susceptibility to psoriasis.Cell death and differentiation · 2026Article
- Microtubule-Associated Proteins: From Dynamic Regulation of Microtubules to Cellular Architecture.Cells · 2026Review
- Phosphorylation remodels the mitotic centrosome matrix to generate bipartite γ-tubulin complex docking sites.Science advances · 2026Article
- Structural basis of human γTuRC closure during CM1-activated microtubule nucleation.Nature communications · 2026Article
- Phosphorylation remodels the mitotic centrosome matrix to generate bipartite γ-tubulin complex docking sites.bioRxiv : the preprint server for biology · 2025Article
- Structural insights into the interplay between microtubule polymerases, γ-tubulin complexes and their receptors.Nature communications · 2025Article
- Proteome-wide forced interactions reveal a functional map of cell-cycle phospho-regulation inNucleus (Austin, Tex.) · 2024Article
- The core spindle pole body scaffold Ppc89 links the pericentrin orthologue Pcp1 to the fission yeast spindle pole body via an evolutionarily conserved interface.Molecular biology of the cell · 2024Article
- Structure of the native γ-tubulin ring complex capping spindle microtubules.Nature structural & molecular biology · 2024Article
- Multifaceted modes of γ-tubulin complex recruitment and microtubule nucleation at mitotic centrosomes.The Journal of cell biology · 2023Article
- Autoinhibitory mechanism controls binding of centrosomin motif 1 to γ-tubulin ring complex.The Journal of cell biology · 2023Article
- Article
- Microtubule nucleation and γTuRC centrosome localization in interphase cells require ch-TOG.Nature communications · 2023Article
- Phosphosites of the yeast centrosome component Spc110 contribute to cell cycle progression and mitotic exit.Biology open · 2022Article
- How Microtubules Build the Spindle Branch by Branch.Annual review of cell and developmental biology · 2022Review
- Pcp1/pericentrin controls the SPB number in fission yeast meiosis and ploidy homeostasis.The Journal of cell biology · 2022Article
- Autoinhibition of Cnn binding to γ-TuRCs prevents ectopic microtubule nucleation and cell division defects.The Journal of cell biology · 2021Article
- Condensation of pericentrin proteins in human cells illuminates phase separation in centrosome assembly.Journal of cell science · 2021Article
- Molecular insight into how γ-TuRC makes microtubules.Journal of cell science · 2021Review
- CM1-driven assembly and activation of yeast γ-tubulin small complex underlies microtubule nucleation.eLife · 2021Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Budding yeast Spc110, a member of γ-tubulin complex receptor family (γ-TuCR), recruits γ-tubulin complexes to microtubule (MT) organizing centers (MTOCs). Biochemical studies suggest that Spc110 facilitates higher-order γ-tubulin complex assembly (Kollman et al., 2010). Nevertheless the molecular basis for this activity and the regulation are unclear. Here we show that Spc110 phosphorylated by Mps1 and Cdk1 activates γ-TuSC oligomerization and MT nucleation in a cell cycle dependent manner. Interaction between the N-terminus of the γ-TuSC subunit Spc98 and Spc110 is important for this activity. Besides the conserved CM1 motif in γ-TuCRs (Sawin et al., 2004), a second motif that we named Spc110/Pcp1 motif (SPM) is also important for MT nucleation. The activating Mps1 and Cdk1 sites lie between SPM and CM1 motifs. Most organisms have both SPM-CM1 (Spc110/Pcp1/PCNT) and CM1-only (Spc72/Mto1/Cnn/CDK5RAP2/myomegalin) types of γ-TuCRs. The two types of γ-TuCRs contain distinct but conserved C-terminal MTOC targeting domains.DOI: http://dx.doi.org/10.7554/eLife.02208.001.
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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.