ArticleMolecular biology of the cell2003
Characterization of a new gammaTuRC subunit with WD repeats.
Article in Molecular biology of the cell, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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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.
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Who cites it
29 citing papers in PubMed, 60 citations in OpenAlex.
- The Warburg micro syndrome protein RAB3GAP1 modulates neuronal morphogenesis and interacts with axon elongation end ER-Golgi trafficking factors.Neurobiology of disease · 2023Article
- TACC3-ch-TOG interaction regulates spindle microtubule assembly by controlling centrosomal recruitment of γ-TuRC.Bioscience reports · 2023Article
- NEDD1-S411 phosphorylation plays a critical function in the coordination of microtubule nucleation during mitosis.Biology open · 2022Article
- How Microtubules Build the Spindle Branch by Branch.Annual review of cell and developmental biology · 2022Review
- Review
- Molecular insight into how γ-TuRC makes microtubules.Journal of cell science · 2021Review
- Microtubule nucleation by γ-tubulin complexes and beyond.Essays in biochemistry · 2018Review
- Assembly and regulation of γ-tubulin complexes.Open biology · 2018Review
- Expression of the novel maternal centrosome assembly factor Wdr8 is required for vertebrate embryonic mitoses.Nature communications · 2017Article
- Functional Analysis of γ-Tubulin Complex Proteins Indicates Specific Lateral Association via Their N-terminal Domains.The Journal of biological chemistry · 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
- Amorphous no more: subdiffraction view of the pericentriolar material architecture.Trends in cell biology · 2014Review
- Fission yeast MOZART1/Mzt1 is an essential γ-tubulin complex component required for complex recruitment to the microtubule organizing center, but not its assembly.Molecular biology of the cell · 2013Article
- Centrosome dysfunction contributes to chromosome instability, chromoanagenesis, and genome reprograming in cancer.Frontiers in oncology · 2013Review
- Dgp71WD is required for the assembly of the acentrosomal Meiosis I spindle, and is not a general targeting factor for the γ-TuRC.Biology open · 2012Article
- Microtubule nucleation by γ-tubulin complexes.Nature reviews. Molecular cell biology · 2011Review
- In vivo analysis of the functions of gamma-tubulin-complex proteins.Journal of cell science · 2009Article
- The WD40 repeat protein NEDD1 functions in microtubule organization during cell division in Arabidopsis thaliana.The Plant cell · 2009Article
- Evaluating the microtubule cytoskeleton and its interacting proteins in monocots by mining the rice genome.Annals of botany · 2009Review
- gammaTub23C interacts genetically with brahma chromatin-remodeling complexes in Drosophila melanogaster.Genetics · 2008Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The gamma-tubulin ring complex (gammaTuRC), consisting of multiple protein subunits, can nucleate microtubule assembly. Although many subunits of the gammaTuRC have been identified, a complete set remains to be defined in any organism. In addition, how the subunits interact with each other to assemble into gammaTuRC remains largely unknown. Here, we report the characterization of a novel gammaTuRC subunit, Drosophila gamma ring protein with WD repeats (Dgp71WD). With the exception of gamma-tubulin, Dgp71WD is the only gammaTuRC component identified to date that does not contain the grip motifs, which are signature sequences conserved in gammaTuRC components. By performing immunoprecipitations after pair-wise coexpression in Sf9 cells, we show that Dgp71WD directly interacts with the grip motif-containing gammaTuRC subunits, Dgrips84, 91, 128, and 163, suggesting that Dgp71WD may play a scaffolding role in gammaTuRC organization. We also show that Dgrips128 and 163, like Dgrips84 and 91, can interact directly with gamma-tubulin. Coexpression of any of these grip motif-containing proteins with gamma-tubulin promotes gamma-tubulin binding to guanine nucleotide. In contrast, in the same assay Dgp71WD interacts with gamma-tubulin but does not facilitate nucleotide binding.
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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.