Interaction of Antiparallel Microtubules in the Phragmoplast Is Mediated by the Microtubule-Associated Protein MAP65-3 in Arabidopsis

In plant cells, microtubules (MTs) in the cytokinetic apparatus phragmoplast exhibit an antiparallel array and transport Golgi-derived vesicles toward MT plus ends located at or near the division site. By transmission electron microscopy, we observed that certain antiparallel phragmoplast MTs overla...

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Bibliographic Details
Published in:The Plant cell 2011-08, Vol.23 (8), p.2909-2923
Main Authors: Ho, Chin-Min Kimmy, Hotta, Takashi, Guo, Fengli, Roberson, Robert W., Lee, Yuh-Ru Julie, Liu, Bo
Format: Article
Language:English
Subjects:
Anaphase
Animals
Antibodies
Arabidopsis - genetics
Arabidopsis - physiology
Arabidopsis - ultrastructure
Arabidopsis Proteins - genetics
Arabidopsis Proteins - metabolism
Bundling
Cell lines
Cytokinesis
Cytokinesis - physiology
Delta cells
Dendritic cells
Escherichia coli - genetics
Escherichia coli - metabolism
Fluorescent antibody techniques
Gene Expression Regulation, Plant
Kinesin - genetics
Kinesin - metabolism
Mice
Microtubule Proteins - metabolism
Microtubule-Associated Proteins - genetics
Microtubule-Associated Proteins - metabolism
Microtubules
Microtubules - physiology
Microtubules - ultrastructure
Mutation
Plant cells
Plant Leaves - genetics
Plant Leaves - physiology
Plant Leaves - ultrastructure
Plant Roots - genetics
Plant Roots - physiology
Plant Roots - ultrastructure
Plants, Genetically Modified
Protein Transport
Rabbits
Recombinant Fusion Proteins
Seedlings - genetics
Seedlings - physiology
Seedlings - ultrastructure
Spindle Apparatus - physiology
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Summary:In plant cells, microtubules (MTs) in the cytokinetic apparatus phragmoplast exhibit an antiparallel array and transport Golgi-derived vesicles toward MT plus ends located at or near the division site. By transmission electron microscopy, we observed that certain antiparallel phragmoplast MTs overlapped and were bridged by electron-dense materials in Arabidopsis thaliana. Robust MT polymerization, reported by fluorescently tagged End Binding"! took place in the phragmoplast midline. The engagement of antiparallel MTs in the central spindle and phragmoplast was largely abolished in mutant cells lacking the MT-associated protein, MAP65-3. We found that endogenous MAP65-3 was selectively detected on the middle segments of the central spindle MTs at late anaphase. When MTs exhibited a bipolar appearance with their plus ends placed in the middle, MAP65-3 exclusively decorated the phragmoplast midline. A bacterially expressed MAP65-3 protein was able to establish the interdigitation of MTs in vitro. MAP65-3 interacted with antiparallel microtubules before motor Kinesin-12 did during the establishment of the phragmoplast MT array. Thus, MAP65-3 selectively crosslinked interdigitating MTs (IMTs) to allow antiparallel MTs to be closely engaged in the phragmoplast. Although the presence of IMTs was not essential for vesicle trafficking, they were required for the phragmoplast-specific motors Kinesin-12 and Phragmoplast-Associated Kinesin-Related Protein2 to interact with MT plus ends. In conclusion, we suggest that the phragmoplast contains IMTs and highly dynamic noninterdigitating MTs, which work in concert to bring about cytokinesis in plant cells.
ISSN:1040-4651
1532-298X
DOI:10.1105/tpc.110.078204