Control of the Atmap65-1 Interaction with Microtubules Through the Cell Cycle.
From: The Integrative Cell Biology Laboratory, School of Biological and Biomedical Sciences, University of Durham, South Road, Durham, DH1 3LE, UK.
Journal of cell science
- Publish Date: Aug 2006
- ISSN: 0021-9533
- Volume: 119
- Issue: Pt 15
- Pages: 3227-37
- Medium: Print
- Language: English
- Citation (JAMA): Smertenko Andrei P, Chang Hsin-Yu, Sonobe Seiji, et al. Control of the Atmap65-1 Interaction with Microtubules Through the Cell Cycle.. J. Cell. Sci. Aug 2006;119:3227-37
Abstract
Cell division depends on the fine control of both microtubule dynamics and microtubule organisation. The microtubule bundling protein MAP65 is a ;midzone MAP’ essential for the integrity of the anaphase spindle and cell division. Arabidopsis thaliana MAP65-1 (AtMAP65-1) binds and bundles microtubules by forming 25 nm cross-bridges. Moreover, as AtMAP65-1 bundles microtubules in interphase, anaphase and telophase but does not bind microtubules in prophase or metaphase, its activity through the cell cycle must be under tight control. Here we show that AtMAP65-1 is hyperphosphorylated during prometaphase and metaphase and that CDK and MAPK are involved in this phosphorylation. This phosphorylation inhibits AtMAP65-1 activity. Expression of non-phosphorylatable AtMAP65-1 has a negative effect on mitotic progression resulting in excessive accumulation of microtubules in the metaphase spindle midzone causing a delay in mitosis. We conclude that normal metaphase spindle organisation and the transition to anaphase is dependent on inactivation of AtMAP65-1.
Mesh Headings (Keywords): Arabidopsis, Arabidopsis Proteins, Cell Cycle, Cells, Cultured, Cyclin-Dependent Kinases, Fluorescence Recovery After Photobleaching, Microtubule-Associated Proteins, Microtubules, Mitogen-Activated Protein Kinases, Mitotic Spindle Apparatus, Peptide Fragments, Phosphorylation, Recombinant Fusion Proteins, Signal Transduction, Tobacco
Check for Full Text / PubMed Unique Identifier (PMID): 16847052
This abstract is part of PubMed, a service of the U.S. National Library of Medicine. PubMed includes more than 17 million citations from MEDLINE and other life science journals for biomedical articles. See Copyright and Disclaimers.
Linked medical terms appearing on this page are added by Healia to help readers find more information and are not part of the original PubMed document.
The data herein was last updated on July 8th, 2008 and may not reflect the most current and accurate data available from NLM.