Microtubule organization across cell types and states

2021 ◽  
Vol 31 (10) ◽  
pp. R506-R511
Author(s):  
Maria D. Sallee ◽  
Jessica L. Feldman
Keyword(s):  
Cell Types ◽  
Microtubule Organization

scholarly journals Lis1 is essential for cortical microtubule organization and desmosome stability in the epidermis

2011 ◽  
Vol 194 (4) ◽  
pp. 631-642 ◽  
Author(s):  
Kaelyn D. Sumigray ◽  
Hsin Chen ◽  
Terry Lechler
Keyword(s):  
Cortical Microtubule ◽  
Cell Types ◽  
Epidermal Differentiation ◽  
Cell Cortex ◽  
Microtubule Organization ◽  
Specific Subset ◽  
Keratin Filaments ◽  
Perinatal Lethality ◽  
Cytoskeletal Networks ◽  
Centrosomal Proteins

Desmosomes are cell–cell adhesion structures that integrate cytoskeletal networks. In addition to binding intermediate filaments, the desmosomal protein desmoplakin (DP) regulates microtubule reorganization in the epidermis. In this paper, we identify a specific subset of centrosomal proteins that are recruited to the cell cortex by DP upon epidermal differentiation. These include Lis1 and Ndel1, which are centrosomal proteins that regulate microtubule organization and anchoring in other cell types. This recruitment was mediated by a region of DP specific to a single isoform, DPI. Furthermore, we demonstrate that the epidermal-specific loss of Lis1 results in dramatic defects in microtubule reorganization. Lis1 ablation also causes desmosomal defects, characterized by decreased levels of desmosomal components, decreased attachment of keratin filaments, and increased turnover of desmosomal proteins at the cell cortex. This contributes to loss of epidermal barrier activity, resulting in completely penetrant perinatal lethality. This work reveals essential desmosome-associated components that control cortical microtubule organization and unexpected roles for centrosomal proteins in epidermal function.

scholarly journals Ste20-related Protein Kinase LOSK (SLK) Controls Microtubule Radial Array in Interphase

2008 ◽  
Vol 19 (5) ◽  
pp. 1952-1961 ◽  
Author(s):  
Anton V. Burakov ◽  
Olga N. Zhapparova ◽  
Olga V. Kovalenko ◽  
Liudmila A. Zinovkina ◽  
Ekaterina S. Potekhina ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Golgi Complex ◽  
Cell Types ◽  
Vero Cells ◽  
Dominant Negative ◽  
Dominant Negative Mutant ◽  
Cellular Regulation ◽  
Microtubule Organization ◽  
Microtubule Stabilization ◽  
Interphase Cells

Interphase microtubules are organized into a radial array with centrosome in the center. This organization is a subject of cellular regulation that can be driven by protein phosphorylation. Only few protein kinases that regulate microtubule array in interphase cells have been described. Ste20-like protein kinase LOSK (SLK) was identified as a microtubule and centrosome-associated protein. In this study we have shown that the inhibition of LOSK activity by dominant-negative mutant K63R-ΔT or by LOSK depletion with RNAi leads to unfocused microtubule arrangement. Microtubule disorganization is prominent in Vero, CV-1, and CHO-K1 cells but less distinct in HeLa cells. The effect is a result neither of microtubule stabilization nor of centrosome disruption. In cells with suppressed LOSK activity centrosomes are unable to anchor or to cap microtubules, though they keep nucleating microtubules. These centrosomes are depleted of dynactin. Vero cells overexpressing K63R-ΔT have normal dynactin “comets” at microtubule ends and unaltered morphology of Golgi complex but are unable to polarize it at the wound edge. We conclude that protein kinase LOSK is required for radial microtubule organization and for the proper localization of Golgi complex in various cell types.

scholarly journals Kinetics and intermediates of marginal band reformation: evidence for peripheral determinants of microtubule organization.

1984 ◽  
Vol 99 (1) ◽  
pp. 70s-75s ◽  
Author(s):  
M Miller ◽  
F Solomon
Keyword(s):  
Cell Types ◽  
Microtubule Assembly ◽  
Cell Periphery ◽  
Microtubule Organizing Center ◽  
Microtubule Organization ◽  
Mature Erythrocyte ◽  
The Reformation ◽  
Marginal Band ◽  
Organizing Center

The microtubules of the mature erythrocyte of the chicken are confined to a band at the periphery. Whole-mount electron microscopy after extraction reveals that the number of microtubules in each cell is almost the same. All the microtubules can be depolymerized by incubation in the cold, and the marginal band can be quantitatively and qualitatively reformed by return to 39 degrees C. These properties allow the reformation of the marginal band to be treated as an in vivo microtubule assembly reaction. The kinetics of this reaction and the intermediates detected during reformation suggest a mechanism of microtubule organization that is distinct from that observed in other cell types. Apparently only one or two growing microtubule ends are available for assembly--assembly is only detected at the cell periphery, even at early times--and there is no evidence of the participation of a microtubule-organizing center.

Cellular Logistics: Unraveling the Interplay Between Microtubule Organization and Intracellular Transport

2019 ◽  
Vol 35 (1) ◽  
pp. 29-54 ◽  
Author(s):  
Mithila Burute ◽  
Lukas C. Kapitein
Keyword(s):  
Intracellular Transport ◽  
Spatial Organization ◽  
Animal Cell ◽  
Cell Types ◽  
Microtubule Organization ◽  
Microtubule Network ◽  
Core Components ◽  
Cell Type Specific ◽  
Microtubule Networks ◽  
Different Cell Types

Microtubules are core components of the cytoskeleton and serve as tracks for motor protein–based intracellular transport. Microtubule networks are highly diverse across different cell types and are believed to adapt to cell type–specific transport demands. Here we review how the spatial organization of different subsets of microtubules into higher-order networks determines the traffic rules for motor-based transport in different animal cell types. We describe the interplay between microtubule network organization and motor-based transport within epithelial cells, oocytes, neurons, cilia, and the spindle apparatus.

scholarly journals Exportin Crm1 is repurposed as a docking protein to generate microtubule organizing centers at the nuclear pore

eLife ◽  
2018 ◽  
Vol 7 ◽  
Author(s):  
Xun X Bao ◽  
Christos Spanos ◽  
Tomoko Kojidani ◽  
Eric M Lynch ◽  
Juri Rappsilber ◽  
...  
Keyword(s):  
Nuclear Export ◽  
Nuclear Export Signal ◽  
Cell Types ◽  
Bound State ◽  
Nuclear Pore ◽  
Nuclear Pore Complexes ◽  
Cytoplasmic Protein ◽  
Microtubule Organization ◽  
Microtubule Organizing Centers ◽  
Pore Complexes

Non-centrosomal microtubule organizing centers (MTOCs) are important for microtubule organization in many cell types. In fission yeast Schizosaccharomyces pombe, the protein Mto1, together with partner protein Mto2 (Mto1/2 complex), recruits the γ-tubulin complex to multiple non-centrosomal MTOCs, including the nuclear envelope (NE). Here, we develop a comparative-interactome mass spectrometry approach to determine how Mto1 localizes to the NE. Surprisingly, we find that Mto1, a constitutively cytoplasmic protein, docks at nuclear pore complexes (NPCs), via interaction with exportin Crm1 and cytoplasmic FG-nucleoporin Nup146. Although Mto1 is not a nuclear export cargo, it binds Crm1 via a nuclear export signal-like sequence, and docking requires both Ran in the GTP-bound state and Nup146 FG repeats. In addition to determining the mechanism of MTOC formation at the NE, our results reveal a novel role for Crm1 and the nuclear export machinery in the stable docking of a cytoplasmic protein complex at NPCs.

scholarly journals A transgenic toolkit for visualizing and perturbing microtubules in mice reveals unexpected functions for non-centrosomal arrays in epidermal morphogenesis

2017 ◽  
Author(s):  
Andrew Muroyama ◽  
Terry Lechler
Keyword(s):  
Cell Types ◽  
Microtubule Dynamics ◽  
Microtubule Organization ◽  
Strong Suppression ◽  
Physiological Functions ◽  
Microtubule Growth ◽  
Epidermal Morphogenesis ◽  
Dynamics And Function ◽  
And Function

AbstractDifferentiation induces reorganization of microtubules (MTs) into non-centrosomal arrays in a variety of tissues. The physiological functions of these microtubule arrays are just beginning to be understood as few tools currently exist to genetically perturb microtubule organization in vivo, particularly in mammals. We developed a genetic toolkit that can be broadly applied to the study of microtubule dynamics and function in many cell types. Using a TRE-EB1-GFP mouse we demonstrate that distinct differentiation transitions in the epidermis cause a decrease in microtubule growth rates and microtubule growth lifetimes, resulting in strong suppression of dynamics. To understand the physiological functions of these stable, non-centrosomal microtubules, we generated a TRE-spastin mouse, which can be used to perturb microtubule organization in a wide-variety of tissues in vivo. Unexpectedly, microtubule perturbation exclusively in post-mitotic keratinocytes had profound consequences on epidermal morphogenesis. We uncoupled novel cell-autonomous roles for MTs in differentiation-driven cell flattening from non-cell autonomous functions in regulating proliferation, differentiation, and tissue architecture. Taken together, we have created tools that will be broadly useful for the study of microtubule dynamics and function in mammalian tissue physiology and have used them to uncover previously unknown functions for non-centrosomal microtubules during mammalian epidermal development.

scholarly journals Giant axonal neuropathy: a conditional mutation affecting cytoskeletal organization.

1985 ◽  
Vol 100 (1) ◽  
pp. 245-250 ◽  
Author(s):  
M W Klymkowsky ◽  
D J Plummer
Keyword(s):  
Culture Media ◽  
Axonal Neuropathy ◽  
Calf Serum ◽  
Cell Types ◽  
Serum Starvation ◽  
Giant Axonal Neuropathy ◽  
Microtubule Organization ◽  
Cytoskeletal Organization ◽  
Recessive Mutations ◽  
Nonpermissive Condition

Giant axonal neuropathy (GAN) results from autosomal recessive mutations (gan-) that affect cytoskeletal organization; specifically, intermediate filaments (IFs) are found collapsed into massive bundles in a variety of different cell types. We studied the gan- fibroblast lines WG321 and WG139 derived from different GAN patients. Although previous studies implied that the gan- IF phenotype was constitutive, we find that it is conditional. That is, when cells were grown under the permissive condition of medium containing over 2% fetal calf serum, most cells had normal IF organization. IF bundles formed when gan- cells were transferred to the nonpermissive condition of low (0.1%) serum. Microtubule organization appeared normal in the presence or absence of serum. The effect of serum starvation was largely blocked or reversed by the addition of BSA to the culture media. We found no evidence that the gan- phenotype depends upon progress through the cell cycle. We discuss the possible role of serum effects in the etiology of GAN and speculate as to the molecular nature of the gan- defect.

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