ArticlePlant physiology2017
Phosphorylation of MAP65-1 by Arabidopsis Aurora Kinases Is Required for Efficient Cell Cycle Progression.
Article in Plant physiology, 2017. 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, 58 citations in OpenAlex.
- Cellular dynamics and molecular signaling networks of plant cytokinesis.Molecules and cells · 2026Review
- Class II kinesin-12 facilitates cell plate formation by transporting cell plate materials in the phragmoplast.Nature plants · 2025Article
- Regulation of cytoskeleton dynamics and its interplay with force in plant cells.Biophysics reviews · 2024Review
- Arabidopsis α-Aurora kinase plays a role in cytokinesis through regulating MAP65-3 association with microtubules at phragmoplast midzone.Nature communications · 2024Article
- New Epigenetic Modifier Inhibitors Enhance Microspore Embryogenesis in Bread Wheat.Plants (Basel, Switzerland) · 2024Article
- Novel inhibitors of microtubule organization and phragmoplast formation in diverse plant species.Life science alliance · 2023Article
- Cortical microtubules contribute to division plane positioning during telophase in maize.The Plant cell · 2023Article
- Microtubule Regulation in Plants: From Morphological Development to Stress Adaptation.Biomolecules · 2023Review
- Plant lineage-specific PIKMIN1 drives APC/CCCS52A2 E3-ligase activity-dependent cell division.Plant physiology · 2023Article
- AUR1 and its pals: orchestration of intracellular rhizobia infection in legume for nitrogen fixation.Plant cell reports · 2023Article
- Overlapping Localization of MAP65-2, -6, and -7 in Arabidopsis Hypocotyl Cells.microPublication biology · 2023Article
- Intracellular infection by symbiotic bacteria requires the mitotic kinase AURORA1.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Protein polarization: Spatiotemporal precisions in cell division and differentiation.Current opinion in plant biology · 2022Review
- Cell biology of primary cell wall synthesis in plants.The Plant cell · 2022Review
- Imaging the living plant cell: From probes to quantification.The Plant cell · 2022Review
- Automated Time-Lapse Imaging and Manipulation of Cell Divisions in Arabidopsis Roots by Vertical-Stage Confocal Microscopy.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Rice microtubule-associated protein OsMAP65-3.1, but not OsMAP65-3.2, plays a critical role in phragmoplast microtubule organization in cytokinesis.Frontiers in plant science · 2022Article
- Comparative transcriptome and DNA methylation analysis in temperature-sensitive genic male sterile wheat BS366.BMC genomics · 2021Article
- Transcriptomes analysis reveals novel insight into the molecular mechanisms of somatic embryogenesis in Hevea brasiliensis.BMC genomics · 2021Article
- The Protein Phosphatase PP2A Plays Multiple Roles in Plant Development by Regulation of Vesicle Traffic-Facts and Questions.International journal of molecular sciences · 2021Review
Corrections and comments
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Authors and funding
15 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aurora kinases are key effectors of mitosis. Plant Auroras are functionally divided into two clades. The alpha Auroras (Aurora1 and Aurora2) associate with the spindle and the cell plate and are implicated in controlling formative divisions throughout plant development. The beta Aurora (Aurora3) localizes to centromeres and likely functions in chromosome separation. In contrast to the wealth of data available on the role of Aurora in other kingdoms, knowledge on their function in plants is merely emerging. This is exemplified by the fact that only histone H3 and the plant homolog of TPX2 have been identified as Aurora substrates in plants. Here we provide biochemical, genetic, and cell biological evidence that the microtubule-bundling protein MAP65-1-a member of the MAP65/Ase1/PRC1 protein family, implicated in central spindle formation and cytokinesis in animals, yeasts, and plants-is a genuine substrate of alpha Aurora kinases. MAP65-1 interacts with Aurora1 in vivo and is phosphorylated on two residues at its unfolded tail domain. Its overexpression and down-regulation antagonistically affect the alpha Aurora double mutant phenotypes. Phospho-mutant analysis shows that Aurora contributes to the microtubule bundling capacity of MAP65-1 in concert with other mitotic kinases.
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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.