Cadherin-Mediated Cell-Cell Adhesion and the Microtubule Network

Gauthier-Rouvière, Cécile; Causeret, Marie; Comunale, Franck; Charrasse, Sophie

doi:10.1007/0-387-28671-3_19

Cited by 4 publications

(2 citation statements)

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“…Most adhesion receptors interact with the cell cytoskeleton through their intracellular domain ( Juliano, 2002 ); LINKIN interacts with microtubules. Microtubules are known to play important functions in cell migration and tissue organization ( Gauthier-Rouvière et al, 2004 ; Etienne-Manneville, 2013 ). They provide structure and rigidity to tissues so that they can withstand high compression forces ( Brangwynne et al, 2007 ), and the bundled cortical microtubules of gonadal cells likely provide such a structure.…”

Section: Discussionmentioning

confidence: 99%

LINKIN, a new transmembrane protein necessary for cell adhesion

Kato

Chou

et al. 2014

eLife

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In epithelial collective migration, leader and follower cells migrate while maintaining cell–cell adhesion and tissue polarity. We have identified a conserved protein and interactors required for maintaining cell adhesion during a simple collective migration in the developing C. elegans male gonad. LINKIN is a previously uncharacterized, transmembrane protein conserved throughout Metazoa. We identified seven atypical FG–GAP domains in the extracellular domain, which potentially folds into a β-propeller structure resembling the α-integrin ligand-binding domain. C. elegans LNKN-1 localizes to the plasma membrane of all gonadal cells, with apical and lateral bias. We identified the LINKIN interactors RUVBL1, RUVBL2, and α-tubulin by using SILAC mass spectrometry on human HEK 293T cells and testing candidates for lnkn-1-like function in C. elegans male gonad. We propose that LINKIN promotes adhesion between neighboring cells through its extracellular domain and regulates microtubule dynamics through RUVBL proteins at its intracellular domain.DOI: http://dx.doi.org/10.7554/eLife.04449.001

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Section: Discussionmentioning

confidence: 99%

LINKIN, a new transmembrane protein necessary for cell adhesion

Kato

Chou

et al. 2014

eLife

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“…Resistant A-431 cells showed an increased amount of β-tubulin, and resistant CAL-39 cells decreased the level of this protein ( Figure 9 ), with an increase in some isotypes ( Supplementary Table S1 ). Microtubules play a role in cell adhesion [ 37 , 38 ], which may promote resistance to various therapies by influencing antiapoptotic pathways [ 7 ]. Additionally, changes in microtubule stability, tubulin isotypes expression and its post-translational modifications have been correlated with poor prognosis and resistance to chemotherapy [ 20 ].…”

Section: Discussionmentioning

confidence: 99%

Possible Mechanisms of Resistance Development to Photodynamic Therapy (PDT) In Vulvar Cancer Cells

Mossakowska

Fabisiewicz

Siedlecki

2022

IJMS

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Photodynamic therapy (PDT) is a low-invasive treatment method that can be used to treat VIN patients. A photosensitizer (PS) applied to a patient is activated with use of the appropriate wavelength of light, which in an oxygen environment leads to the formation of a reactive oxygen species (ROS) that destroys the tumor. However, cells can protect themselves against these cytotoxic products by increasing their antioxidant mechanisms and repair capacity. Changes in the cytoskeleton may also influence resistance to PDT. Our results revealed that PDT-resistant cells changed the amount of ROS. Cells resistant to PDT A-431 exhibited a decreased ROS level and showed higher viability after oxidizing agent treatment. Resistant Cal-39 cells exhibited a decreased O2− level but increased other ROS. This provides protection from PDT but not from other oxidizing agents. Moreover, PDT leads to alterations in the cytoskeleton that may result in an epithelial-mesenchymal transition (EMT) or increased adhesion. Both EMT and cell adhesion may activate signaling pathways involved in survival. This means that resistance to PDT in vulvar cancer may be at least in part a result of changes in ROS level and alterations in the cytoskeleton.

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