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In vivo dynamics and differential microtubule-binding activities of MAP65 proteins

(2004) PLANT PHYSIOLOGY. 136(4). p.3956-3967
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Abstract
Plant cells produce different microtubule arrays that are essential for cell division and morphogenesis without equivalent in other eukaryotes. Microtubule-associated proteins influence the behavior of microtubules that is presumed to culminate into transitions from one array to another. We analyzed the microtubule-binding properties of three Arabidopsis (Arabidopsis thaliana) members, AtMAP65-1, AtMAP65-4, and AtMAP65-5, in live cells using laser scanning confocal microscopy. Depending on the overall organization of the cortical array, AtMAP65-1-GFP (green fluorescent protein) and AtMAP65-5GFP associated with a subset of microtubules. In cells containing both coaligned and oblique microtubules, AtMAP65-1-GFP and AtMAP65-5-GFP tended to be associated with the coaligned microtubules. Cortical microtubules labeled with AtMAP65-1GFP and AtMAP65-5-GFP appeared as thick bundles and showed more resistance to microtubule-destabilizing drugs. The polymerization rates of AtMAP65-1-GFP and AtMAP65-5-GFP microtubules were similar to those of tubulin-GFP marked microtubules but were different from AtEB1a-GFP, a microtubule plus-end-binding EB1-like protein that stimulated polymerization. By contrast, depolymerization rates of AtMAP65-1-GFP- and AtMAP65-5-GFP-labeled microtubules were reduced. AtMAP65-1-GFP associated with polymerizing microtubules within a bundle, and with fixed microtubule termini, suggesting that AtMAP65-1's function is to bundle and stabilize adjacent microtubules of the cortex. Polymerization within a bundle took place in either direction so that bundling occurred between parallel or antiparallel aligned microtubules. AtMAP65-4-GFP did not label cortical microtubules or the preprophase band, despite continuous expression driven by the 35S promoter, and its subcellular localization was restricted to microtubules that rearranged to form a spindle and the polar sides of the spindle proper. The expression of AtMAP65-4 peaked at mitosis, in agreement with a function related to spindle formation, whereas AtMAP65-1 and AtMAP65-5 were expressed throughout the cell cycle.
Keywords
SUSPENSION, CYTOSKELETON, VITRO, INSTABILITY, ORGANIZATION, ARABIDOPSIS, FLUORESCENT PROTEIN, PLANT-CELLS, CYCLE-DEPENDENT PROTEOLYSIS, TOBACCO BY-2 CELLS

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MLA
Van Damme, Daniël, Kris Van Poucke, Emmanuel Boutant, et al. “In Vivo Dynamics and Differential Microtubule-binding Activities of MAP65 Proteins.” PLANT PHYSIOLOGY 136.4 (2004): 3956–3967. Print.
APA
Van Damme, Daniël, Van Poucke, K., Boutant, E., Ritzenthaler, C., Inzé, D., & Geelen, D. (2004). In vivo dynamics and differential microtubule-binding activities of MAP65 proteins. PLANT PHYSIOLOGY, 136(4), 3956–3967.
Chicago author-date
Van Damme, Daniël, Kris Van Poucke, Emmanuel Boutant, Christophe Ritzenthaler, Dirk Inzé, and Danny Geelen. 2004. “In Vivo Dynamics and Differential Microtubule-binding Activities of MAP65 Proteins.” Plant Physiology 136 (4): 3956–3967.
Chicago author-date (all authors)
Van Damme, Daniël, Kris Van Poucke, Emmanuel Boutant, Christophe Ritzenthaler, Dirk Inzé, and Danny Geelen. 2004. “In Vivo Dynamics and Differential Microtubule-binding Activities of MAP65 Proteins.” Plant Physiology 136 (4): 3956–3967.
Vancouver
1.
Van Damme D, Van Poucke K, Boutant E, Ritzenthaler C, Inzé D, Geelen D. In vivo dynamics and differential microtubule-binding activities of MAP65 proteins. PLANT PHYSIOLOGY. 2004;136(4):3956–67.
IEEE
[1]
D. Van Damme, K. Van Poucke, E. Boutant, C. Ritzenthaler, D. Inzé, and D. Geelen, “In vivo dynamics and differential microtubule-binding activities of MAP65 proteins,” PLANT PHYSIOLOGY, vol. 136, no. 4, pp. 3956–3967, 2004.
@article{299722,
  abstract     = {Plant cells produce different microtubule arrays that are essential for cell division and morphogenesis without equivalent in other eukaryotes. Microtubule-associated proteins influence the behavior of microtubules that is presumed to culminate into transitions from one array to another. We analyzed the microtubule-binding properties of three Arabidopsis (Arabidopsis thaliana) members, AtMAP65-1, AtMAP65-4, and AtMAP65-5, in live cells using laser scanning confocal microscopy. Depending on the overall organization of the cortical array, AtMAP65-1-GFP (green fluorescent protein) and AtMAP65-5GFP associated with a subset of microtubules. In cells containing both coaligned and oblique microtubules, AtMAP65-1-GFP and AtMAP65-5-GFP tended to be associated with the coaligned microtubules. Cortical microtubules labeled with AtMAP65-1GFP and AtMAP65-5-GFP appeared as thick bundles and showed more resistance to microtubule-destabilizing drugs. The polymerization rates of AtMAP65-1-GFP and AtMAP65-5-GFP microtubules were similar to those of tubulin-GFP marked microtubules but were different from AtEB1a-GFP, a microtubule plus-end-binding EB1-like protein that stimulated polymerization. By contrast, depolymerization rates of AtMAP65-1-GFP- and AtMAP65-5-GFP-labeled microtubules were reduced. AtMAP65-1-GFP associated with polymerizing microtubules within a bundle, and with fixed microtubule termini, suggesting that AtMAP65-1's function is to bundle and stabilize adjacent microtubules of the cortex. Polymerization within a bundle took place in either direction so that bundling occurred between parallel or antiparallel aligned microtubules. AtMAP65-4-GFP did not label cortical microtubules or the preprophase band, despite continuous expression driven by the 35S promoter, and its subcellular localization was restricted to microtubules that rearranged to form a spindle and the polar sides of the spindle proper. The expression of AtMAP65-4 peaked at mitosis, in agreement with a function related to spindle formation, whereas AtMAP65-1 and AtMAP65-5 were expressed throughout the cell cycle.},
  author       = {Van Damme, Daniël and Van Poucke, Kris and Boutant, Emmanuel and Ritzenthaler, Christophe and Inzé, Dirk and Geelen, Danny},
  issn         = {0032-0889},
  journal      = {PLANT PHYSIOLOGY},
  keywords     = {SUSPENSION,CYTOSKELETON,VITRO,INSTABILITY,ORGANIZATION,ARABIDOPSIS,FLUORESCENT PROTEIN,PLANT-CELLS,CYCLE-DEPENDENT PROTEOLYSIS,TOBACCO BY-2 CELLS},
  language     = {eng},
  number       = {4},
  pages        = {3956--3967},
  title        = {In vivo dynamics and differential microtubule-binding activities of MAP65 proteins},
  url          = {http://dx.doi.org/10.1104/pp.104.051623},
  volume       = {136},
  year         = {2004},
}

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