ArticleMolecular biology of the cell2004
Megator, an essential coiled-coil protein that localizes to the putative spindle matrix during mitosis in Drosophila.
Article in Molecular biology of the cell, 2004. 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.
- NPP-21/TPR is required for developmental control of spindle checkpoint strength inbioRxiv : the preprint server for biology · 2026Article
- Identification of a cytosol-to-nucleus feedback loop that regulates neuronal microtubule nucleation.The Journal of cell biology · 2026Article
- A non-transcriptional mitotic function of POU/Oct factors ensures spindle assembly and chromosome segregation.Journal of cell science · 2026Article
- Sustainable integrative cell biology: CENP-C is guilty by association.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2025Article
- Article
- Fission yeast essential nuclear pore protein Nup211 regulates the expression of genes involved in cytokinesis.PloS one · 2024Article
- You are who your friends are-nuclear pore proteins as components of chromatin-binding complexes.FEBS letters · 2023Review
- The microtubule- and PP1-binding activities ofMolecular biology of the cell · 2022Article
- Correct dosage of X chromosome transcription is controlled by a nuclear pore component.Cell reports · 2021Article
- Mps1-mediated release of Mad1 from nuclear pores ensures the fidelity of chromosome segregation.The Journal of cell biology · 2020Article
- Article
- Evidence for a role of spindle matrix formation in cell cycle progression by antibody perturbation.PloS one · 2018Article
- Comparative interactomics provides evidence for functional specialization of the nuclear pore complex.Nucleus (Austin, Tex.) · 2017Article
- The Nuclear Matrix Protein Megator Regulates Stem Cell Asymmetric Division through the Mitotic Checkpoint Complex in Drosophila Testes.PLoS genetics · 2015Article
- Article
- An organelle-exclusion envelope assists mitosis and underlies distinct molecular crowding in the spindle region.The Journal of cell biology · 2015Article
- Concentrating on the mitotic spindle.The Journal of cell biology · 2015Article
- Control of the spindle checkpoint by lateral kinetochore attachment and limited Mad1 recruitment.Molecular biology of the cell · 2015Article
- The nucleoporin Mlp2 is involved in chromosomal distribution during mitosis in trypanosomatids.Nucleic acids research · 2015Article
- Patterns of positive selection in seven ant genomes.Molecular biology and evolution · 2014Article
Corrections and comments
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Authors and funding
11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have used immunocytochemistry and cross-immunoprecipitation analysis to demonstrate that Megator (Bx34 antigen), a Tpr ortholog in Drosophila with an extended coiled-coil domain, colocalizes with the putative spindle matrix proteins Skeletor and Chromator during mitosis. Analysis of P-element mutations in the Megator locus showed that Megator is an essential protein. During interphase Megator is localized to the nuclear rim and occupies the intranuclear space surrounding the chromosomes. However, during mitosis Megator reorganizes and aligns together with Skeletor and Chromator into a fusiform spindle structure. The Megator metaphase spindle persists in the absence of microtubule spindles, strongly implying that the existence of the Megator-defined spindle does not require polymerized microtubules. Deletion construct analysis in S2 cells indicates that the COOH-terminal part of Megator without the coiled-coil region was sufficient for both nuclear as well as spindle localization. In contrast, the NH2-terminal coiled-coil region remains in the cytoplasm; however, we show that it is capable of assembling into spherical structures. On the basis of these findings we propose that the COOH-terminal domain of Megator functions as a targeting and localization domain, whereas the NH2-terminal domain is responsible for forming polymers that may serve as a structural basis for the putative spindle matrix complex.
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