scholarly journals Submembraneous microtubule cytoskeleton: interaction of TRPP2 with the cell cytoskeleton

FEBS Journal ◽  
2008 ◽  
Vol 275 (19) ◽  
pp. 4675-4683 ◽  
Author(s):  
Xing-Zhen Chen ◽  
Qiang Li ◽  
Yuliang Wu ◽  
Genqing Liang ◽  
Carlos J. Lara ◽  
...  
Keyword(s):  
Microtubule Cytoskeleton ◽  
Cell Cytoskeleton

scholarly journals Differential requirement of F-actin and microtubule cytoskeleton in cue-induced local protein synthesis in axonal growth cones

2015 ◽  
Vol 10 (1) ◽  
pp. 3 ◽  
Author(s):  
Michael Piper ◽  
Aih Lee ◽  
Francisca van Horck ◽  
Heather McNeilly ◽  
Trina Lu ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Axonal Growth ◽  
Growth Cones ◽  
Microtubule Cytoskeleton ◽  
Local Protein Synthesis ◽  
Local Protein

scholarly journals Lignans from Bursera fagaroides Affect In Vivo Cell Behavior by Disturbing the Tubulin Cytoskeleton in Zebrafish Embryos

Molecules ◽  
2018 ◽  
Vol 24 (1) ◽  
pp. 8 ◽  
Author(s):  
Mayra Antúnez-Mojica ◽  
Andrés Rojas-Sepúlveda ◽  
Mario Mendieta-Serrano ◽  
Leticia Gonzalez-Maya ◽  
Silvia Marquina ◽  
...  
Keyword(s):  
Cell Migration ◽  
Biological Effects ◽  
In Vitro Models ◽  
In Vivo Model ◽  
Zebrafish Embryos ◽  
Microtubule Cytoskeleton ◽  
Zebrafish Model ◽  
Bioassay Guided Fractionation

By using a zebrafish embryo model to guide the chromatographic fractionation of antimitotic secondary metabolites, seven podophyllotoxin-type lignans were isolated from a hydroalcoholic extract obtained from the steam bark of Bursera fagaroides. The compounds were identified as podophyllotoxin (1), β-peltatin-A-methylether (2), 5′-desmethoxy-β-peltatin-A-methylether (3), desmethoxy-yatein (4), desoxypodophyllotoxin (5), burseranin (6), and acetyl podophyllotoxin (7). The biological effects on mitosis, cell migration, and microtubule cytoskeleton remodeling of lignans 1–7 were further evaluated in zebrafish embryos by whole-mount immunolocalization of the mitotic marker phospho-histone H3 and by a tubulin antibody. We found that lignans 1, 2, 4, and 7 induced mitotic arrest, delayed cell migration, and disrupted the microtubule cytoskeleton in zebrafish embryos. Furthermore, microtubule cytoskeleton destabilization was observed also in PC3 cells, except for 7. Therefore, these results demonstrate that the cytotoxic activity of 1, 2, and 4 is mediated by their microtubule-destabilizing activity. In general, the in vivo and in vitro models here used displayed equivalent mitotic effects, which allows us to conclude that the zebrafish model can be a fast and cheap in vivo model that can be used to identify antimitotic natural products through bioassay-guided fractionation.

Stress-induced fractal rearrangement of the endothelial cell cytoskeleton causes apoptosis

Surgery ◽  
1998 ◽  
Vol 124 (2) ◽  
pp. 362-371 ◽  
Author(s):  
Susan L. DeMeester ◽  
J.Perren Cobb ◽  
Richard S. Hotchkiss ◽  
Dale F. Osborne ◽  
Irene E. Karl ◽  
...  
Keyword(s):  
Endothelial Cell ◽  
Cell Cytoskeleton

scholarly journals TUBA1A mutations identified in lissencephaly patients dominantly disrupt neuronal migration and impair dynein activity

2018 ◽  
Vol 28 (8) ◽  
pp. 1227-1243 ◽  
Author(s):  
Jayne Aiken ◽  
Jeffrey K Moore ◽  
Emily A Bates
Keyword(s):  
Motor Activity ◽  
Neuronal Migration ◽  
Ectopic Expression ◽  
Missense Mutations ◽  
Microtubule Cytoskeleton ◽  
Tubulin Genes ◽  
Dynein Motor ◽  
Brain Malformations ◽  
Developing Mouse Brain ◽  
And Migration

Abstract The microtubule cytoskeleton supports diverse cellular morphogenesis and migration processes during brain development. Mutations in tubulin genes are associated with severe human brain malformations known as ‘tubulinopathies’; however, it is not understood how molecular-level changes in microtubule subunits lead to brain malformations. In this study, we demonstrate that missense mutations affecting arginine at position 402 (R402) of TUBA1A α-tubulin selectively impair dynein motor activity and severely and dominantly disrupt cortical neuronal migration. TUBA1A is the most commonly affected tubulin gene in tubulinopathy patients, and mutations altering R402 account for 30% of all reported TUBA1A mutations. We show for the first time that ectopic expression of TUBA1A-R402C and TUBA1A-R402H patient alleles is sufficient to dominantly disrupt cortical neuronal migration in the developing mouse brain, strongly supporting a causal role in the pathology of brain malformation. To isolate the precise molecular impact of R402 mutations, we generated analogous R402C and R402H mutations in budding yeast α-tubulin, which exhibit a simplified microtubule cytoskeleton. We find that R402 mutant tubulins assemble into microtubules that support normal kinesin motor activity but fail to support the activity of dynein motors. Importantly, the level of dynein impairment scales with the expression level of the mutant in the cell, suggesting a ‘poisoning’ mechanism in which R402 mutant α-tubulin acts dominantly by populating microtubules with defective binding sites for dynein. Based on our results, we propose a new model for the molecular pathology of tubulinopathies that may also extend to other tubulin-related neuropathies.

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