ArticleThe Journal of cell biology2012
An extended γ-tubulin ring functions as a stable platform in microtubule nucleation.
Article in The Journal of cell biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
31 citing papers in PubMed, 51 citations in OpenAlex.
- Towards Unbiased Fluorophore Counting in Superresolution Fluorescence Microscopy.Nanomaterials (Basel, Switzerland) · 2023Article
- Epistasis, aneuploidy, and functional mutations underlie evolution of resistance to induced microtubule depolymerization.The EMBO journal · 2021Article
- Anatomy of the fungal microtubule organizing center, the spindle pole body.Current opinion in structural biology · 2021Review
- Distribution of γ-tubulin ring complex at themicroPublication biology · 2021Article
- Assembly of the asymmetric human γ-tubulin ring complex by RUVBL1-RUVBL2 AAA ATPase.Science advances · 2020Article
- The role of gene dosage in budding yeast centrosome scaling and spontaneous diploidization.PLoS genetics · 2020Article
- Article
- Article
- Article
- Single-cell profiling screen identifies microtubule-dependent reduction of variability in signaling.Molecular systems biology · 2018Article
- Assembly and regulation of γ-tubulin complexes.Open biology · 2018Review
- Functional Analysis of γ-Tubulin Complex Proteins Indicates Specific Lateral Association via Their N-terminal Domains.The Journal of biological chemistry · 2016Article
- Cytoskeletal impairment during isoamyl alcohol-induced cell elongation in budding yeast.Scientific reports · 2016Article
- Higher-order oligomerization of Spc110p drives γ-tubulin ring complex assembly.Molecular biology of the cell · 2016Article
- Synergistic role of fission yeast Alp16GCP6 and Mzt1MOZART1 in γ-tubulin complex recruitment to mitotic spindle pole bodies and spindle assembly.Molecular biology of the cell · 2016Article
- Article
- Kar1 binding to Sfi1 C-terminal regions anchors the SPB bridge to the nuclear envelope.The Journal of cell biology · 2015Article
- The centrosome and its duplication cycle.Cold Spring Harbor perspectives in biology · 2015Review
- Ring closure activates yeast γTuRC for species-specific microtubule nucleation.Nature structural & molecular biology · 2015Article
- Every laboratory with a fluorescence microscope should consider counting molecules.Molecular biology of the cell · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
γ-Tubulin complexes are essential for microtubule (MT) nucleation. The γ-tubulin small complex (γ-TuSC) consists of two molecules of γ-tubulin and one molecule each of Spc97 and Spc98. In vitro, γ-TuSCs oligomerize into spirals of 13 γ-tubulin molecules per turn. However, the properties and numbers of γ-TuSCs at MT nucleation sites in vivo are unclear. In this paper, we show by fluorescence recovery after photobleaching analysis that γ-tubulin was stably integrated into MT nucleation sites and was further stabilized by tubulin binding. Importantly, tubulin showed a stronger interaction with the nucleation site than with the MT plus end, which probably provides the basis for MT nucleation. Quantitative analysis of γ-TuSCs on single MT minus ends argued for nucleation sites consisting of approximately seven γ-TuSCs with approximately three additional γ-tubulin molecules. Nucleation and anchoring of MTs required the same number of γ-tubulin molecules. We suggest that a spiral of seven γ-TuSCs with a slight surplus of γ-tubulin nucleates MTs in vivo.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.