Microtubule Integrity Is Necessary for the Epithelial Barrier Function of Cultured Thyroid Cell Monolayers

Yap, Alpha S.; Stevenson, Bruce R.; Abel, K C; Cragoe, Edward J.; Manley, S. W.

doi:10.1006/excr.1995.1189

Cited by 47 publications

(41 citation statements)

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“…5). In contrast to the loss of the E-cadherin signal observed after microtubule depolymerization in thyroid monolayers or in CHO cells (Yap et al, 1995;Waterman-Storer et al, 2000;Stehbens et al, 2006), we mainly observed short fragments perpendicular to the plane of the membrane. This phenotype might be caused by the observed E-cadherin mobility defects.…”

Section: Microtubules Promote Adherens Junction Integritycontrasting

confidence: 88%

Non-centrosomal epidermal microtubules act in parallel to LET-502/ROCK to promote C. elegans elongation

Quintin¹,

Wang²,

Pontabry³

et al. 2016

Journal of Cell Science

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There was an error in Development (2016Development ( ) 143, 160-173 (doi: 10.1242).The first name of the second author was spelled incorrectly. The online version has now been corrected. The authors apologise to readers for this mistake. C. elegans embryonic elongation is a morphogenetic event driven by actomyosin contractility and muscle-induced tension transmitted through hemidesmosomes. A role for the microtubule cytoskeleton has also been proposed, but its contribution remains poorly characterized. Here, we investigate the organization of the noncentrosomal microtubule arrays present in the epidermis and assess their function in elongation. We show that the microtubule regulators γ-tubulin and NOCA-1 are recruited to hemidesmosomes and adherens junctions early in elongation. Several parallel approaches suggest that microtubule nucleation occurs from these sites. Disrupting the epidermal microtubule array by overexpressing the microtubulesevering protein Spastin or by inhibiting the C. elegans ninein homolog NOCA-1 in the epidermis mildly affected elongation. However, microtubules were essential for elongation when hemidesmosomes or the activity of the Rho kinase LET-502/ROCK were partially compromised. Imaging of junctional components and genetic analyses suggest that epidermal microtubules function together with Rho kinase to promote the transport of E-cadherin to adherens junctions and myotactin to hemidesmosomes. Our results indicate that the role of LET-502 in junctional remodeling is likely to be independent of its established function as a myosin II activator, but requires a microtubule-dependent pathway involving the syntaxin SYX-5. Hence, we propose that non-centrosomal microtubules organized by epidermal junctions contribute to elongation by transporting junction remodeling factors, rather than having a mechanical role.

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Section: Microtubules Promote Adherens Junction Integritycontrasting

confidence: 88%

Non-centrosomal epidermal microtubules act in parallel to LET-502/ROCK to promote C. elegans elongation

Quintin¹,

Wang²,

Pontabry³

et al. 2016

Journal of Cell Science

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“…Microtubules, as central elements of the cytoskeleton, play critical roles in the generation of an apico-basolateral polarity and specific transport pathways to the apical or the basolateral cell pole (Müsch, 2004). Alterations in microtubule composition thus affect the integrity of epithelial cell sheets (Yap et al, 1995). Tubulin is subject to distinct post-translational modifications, which include acetylation, tyrosination, detyrosination, D2 modification, polyglutamylation, palmitoylation and phosphorylation (Hammond et al, 2008).…”

Section: Introductionmentioning

confidence: 99%

Tubulin detyrosination promotes monolayer formation and apical trafficking in epithelial cells

Zink

Große

Freikamp

et al. 2012

Journal of Cell Science

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SummaryThe role of post-translational tubulin modifications in the development and maintenance of a polarized epithelium is not well understood. We studied the balance between detyrosinated (detyr-) and tyrosinated (tyr-) tubulin in the formation of MDCK cell monolayers. Increased quantities of detyrosinated microtubules were detected during assembly into confluent cell sheets. These tubules were composed of alternating stretches of detyr-and tyr-tubulin. Constant induction of tubulin tyrosination, which decreased the levels of detyr-tubulin by overexpression of tubulin tyrosine ligase (TTL), disrupted monolayer establishment. Detyr-tubulin-depleted cells assembled into isolated islands and developed a prematurely polarized architecture. Thus, tubulin detyrosination is required for the morphological differentiation from non-polarized cells into an epithelial monolayer. Moreover, membrane trafficking, in particular to the apical domain, was slowed down in TTL-overexpressing cells. This effect could be reversed by TTL knockdown, which suggests that detyr-tubulin-enriched microtubules serve as cytoskeletal tracks to guide membrane cargo in polarized MDCK cells.

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“…Colchicine, a cell microtubule antagonist, was reported to disrupt the microtubule integrity in the cultured thyroid cell monolayer. 45) It was included in the present study with the aim to understand whether colchicine also disrupt the tight junction of HOIEC monolayer. The permeated amount of insulin and the P app value were not significantly enhanced by the colchicines, indicating that colchicines may not affect the tight junction of HOIEC monolayer.…”

Section: Discussionmentioning

confidence: 99%

Sublingual Delivery of Insulin: Effects of Enhancers on the Mucosal Lipid Fluidity and Protein Conformation, Transport, and in Vivo Hypoglycemic Activity

Cui

Lü

Xiao

et al. 2005

Biological & Pharmaceutical Bulletin

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The purposes of this study were to evaluate effects of enhancers for sublingual delivering insulin on the mucosal lipid fluidity and protein conformation, transport, and in vivo hypoglycemic activity in normal rats. The effects on sublingual mucosa, and aggregation states of insulin were estimated using fluorescence polarization, and circular dichroism method, respectively. The human immortalized oral epithelial cell monolayer was used for evaluating transport of insulin. Hydroxylpropyl-b b-cyclodextrin (HP-b b-CD), chitosan, polyethylene-polypropylene glycol, polyoxyethylene lauryl ether, polysorbate 80, egg lecithin, or oleic acid, was used as a penetration enhancer, respectively. The fluidity of sublingual mucosal lipid was markedly reduced by these enhancers excluding polysorbate 80, and the secondary structure of the mucosal proteins was also influenced by these enhancers. The hexamers of insulin were dissociated to monomers only by chitosan, polyoxyethylene lauryl ether, and egg lecithin. Nonetheless, plasma glucose levels in normal rats were significantly lowered after sublingual administration of insulin with an enhancer compared with those without an enhancer at the same time-point. The enhancing effects may be due to one or multiple factors: increasing the mucosal lipid fluidity, directly loosing the tight junction of epithelia, and dissociating the hexamers of insulin to monomers. Among these, the opened tight junction may correlate most with the enhancing effect in the mucosal permeability. Because the aggregates of insulin exist, the dissociation of the aggregates by an enhancer would benefit the permeability.

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Microtubule Integrity Is Necessary for the Epithelial Barrier Function of Cultured Thyroid Cell Monolayers

Cited by 47 publications

References 0 publications

Non-centrosomal epidermal microtubules act in parallel to LET-502/ROCK to promote C. elegans elongation

Non-centrosomal epidermal microtubules act in parallel to LET-502/ROCK to promote C. elegans elongation

Tubulin detyrosination promotes monolayer formation and apical trafficking in epithelial cells

Sublingual Delivery of Insulin: Effects of Enhancers on the Mucosal Lipid Fluidity and Protein Conformation, Transport, and in Vivo Hypoglycemic Activity

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