Microtubules Mechanically Regulate Cell Adhesion Strengthening Via Cell Shape

2013 ◽  
Vol 7 (1) ◽  
pp. 136-144 ◽  
Author(s):  
Kranthi Kumar Elineni ◽  
Nathan D. Gallant
Keyword(s):  
Cell Adhesion ◽  
Cell Shape

scholarly journals Layilin, a Novel Integral Membrane Protein, Is a Hyaluronan Receptor

2001 ◽  
Vol 12 (4) ◽  
pp. 891-900 ◽  
Author(s):  
Petri Bono ◽  
Kristofer Rubin ◽  
Jonathan M. G. Higgins ◽  
Richard O. Hynes
Keyword(s):  
Cell Adhesion ◽  
Fusion Protein ◽  
Cell Shape ◽  
Transmembrane Protein ◽  
Adaptor Proteins ◽  
Integral Membrane Protein ◽  
Microtiter Plate ◽  
Binding Assays ◽  
Cellular Processes ◽  
Fc Fusion Protein

The actin cytoskeleton plays a significant role in changes of cell shape and motility, and interactions between the actin filaments and the cell membrane are crucial for a variety of cellular processes. Several adaptor proteins, including talin, maintain the cytoskeleton-membrane linkage by binding to integral membrane proteins and to the cytoskeleton. Layilin, a recently characterized transmembrane protein with homology to C-type lectins, is a membrane-binding site for talin in peripheral ruffles of spreading cells. To facilitate studies of layilin's function, we have generated a layilin-Fc fusion protein comprising the extracellular part of layilin joined to human immunoglobulin G heavy chain and used this chimera to identify layilin ligands. Here, we demonstrate that layilin-Fc fusion protein binds to hyaluronan immobilized to Sepharose. Microtiter plate-binding assays, coprecipitation experiments, and staining of sections predigested with different glycosaminoglycan-degrading enzymes and cell adhesion assays all revealed that layilin binds specifically to hyaluronan but not to other tested glycosaminoglycans. Layilin's ability to bind hyaluronan, a ubiquitous extracellular matrix component, reveals an interesting parallel between layilin and CD44, because both can bind to cytoskeleton-membrane linker proteins through their cytoplasmic domains and to hyaluronan through their extracellular domains. This parallelism suggests a role for layilin in cell adhesion and motility.

scholarly journals A Putative Catenin–Cadherin System Mediates Morphogenesis of the Caenorhabditis elegans Embryo

1998 ◽  
Vol 141 (1) ◽  
pp. 297-308 ◽  
Author(s):  
Michael Costa ◽  
William Raich ◽  
Cristina Agbunag ◽  
Ben Leung ◽  
Jeff Hardin ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Caenorhabditis Elegans ◽  
Cell Shape ◽  
Shape Change ◽  
Adherens Junctions ◽  
The Body ◽  
C Elegans ◽  
Cell Shape Change ◽  
Filament Bundles ◽  
Cell Adhesion Proteins

During morphogenesis of the Caenorhabditis elegans embryo, hypodermal (or epidermal) cells migrate to enclose the embryo in an epithelium and, subsequently, change shape coordinately to elongate the body (Priess, J.R., and D.I. Hirsh. 1986. Dev. Biol. 117:156– 173; Williams-Masson, E.M., A.N. Malik, and J. Hardin. 1997. Development [Camb.]. 124:2889–2901). We have isolated mutants defective in morphogenesis that identify three genes required for both cell migration during body enclosure and cell shape change during body elongation. Analyses of hmp-1, hmp-2, and hmr-1 mutants suggest that products of these genes anchor contractile actin filament bundles at the adherens junctions between hypodermal cells and, thereby, transmit the force of bundle contraction into cell shape change. The protein products of all three genes localize to hypodermal adherens junctions in embryos. The sequences of the predicted HMP-1, HMP-2, and HMR-1 proteins are related to the cell adhesion proteins α-catenin, β-catenin/Armadillo, and classical cadherin, respectively. This putative catenin–cadherin system is not essential for general cell adhesion in the C. elegans embryo, but rather mediates specific aspects of morphogenetic cell shape change and cytoskeletal organization.

scholarly journals MPC-07 MECHANISMS OF BETTER PROGNOSIS IN IDH-MUTATED ASTROCYTOMA WITH 19Q-LOSS

2019 ◽  
Vol 1 (Supplement_2) ◽  
pp. ii23-ii23
Author(s):  
Ryohei Otani ◽  
Takeo Uzuka ◽  
Fumi Higuchi ◽  
Hadzki Matsuda ◽  
Phyo Kim ◽  
...  
Keyword(s):  
Overall Survival ◽  
Cell Adhesion ◽  
Axon Guidance ◽  
Neuronal Differentiation ◽  
Expression Pattern ◽  
Tumor Immunity ◽  
Cell Shape ◽  
Ras Signaling ◽  
Tumor Proliferation ◽  
Ras Signaling Pathway

Abstract We previously reported that there was a subgroup of IDH-mutated astrocytomas harboring only 19q-loss showing oligodendroglioma-like morphology and significantly longer overall survival (OS) compared with 19q-intact astrocytomas (Otani et al. Cancer Sci 2018). The purpose of the present study was to reveal how 19q-loss contributed to better prognosis and the morphology in the subgroup. We compared expression pattern between five 19q-loss and five 19q-intact IDH-mutated astrocytomas by microarray analysis. 136 up-regulated genes and 203 down regulated genes were extracted in 19q-loss astrocytomas compared with 19q-intact astrocytomas. Significantly changed genes distributed throughout all chromosomes, but more down-regulated genes were on 19q and 4p, and more up-regulated genes were on 4q. Genes associated with apoptosis, cell adhesion, and antigen presentation were up-regulated, and genes associated with Ras signaling pathway were down-regulated. These changes could result in better prognosis. By contrast, there was few expression changed gene associated with oligodendroglioma-like morphology although up-regulation of genes associated with axon guidance and down-regulation of genes associated with cell shape might result in the morphology or neuronal differentiation. Expression pattern of 19q-loss astrocytomas indicated no tendency of oligodendroglial differentiation. Better prognosis of 19q-loss astrocytomas was derived from expression changes associated with tumor proliferation and tumor immunity.

scholarly journals Tissue architecture: the ultimate regulator of epithelial function?

1998 ◽  
Vol 353 (1370) ◽  
pp. 857-870 ◽  
Author(s):  
Carmen Hagios ◽  
André Lochter ◽  
Mina J. Bissell
Keyword(s):  
Cell Adhesion ◽  
Cell Shape ◽  
Tissue Structure ◽  
Tissue Architecture ◽  
Cell Behaviour ◽  
Matrix Interactions ◽  
Adhesive Interactions ◽  
And Function ◽  
Extracellular Matrix Interactions

The architecture of a tissue is defined by the nature and the integrity of its cellular and extracellular compartments, and is based on proper adhesive cell–cell and cell–extracellular matrix interactions. Cadherins and integrins are major adhesion–mediators that assemble epithelial cells together laterally and attach them basally to a subepithelial basement membrane, respectively. Because cell adhesion complexes are linked to the cytoskeleton and to the cellular signalling pathways, they represent checkpoints for regulation of cell shape and gene expression and thus are instructive for cell behaviour and function. This organization allows a reciprocal flow of mechanical and biochemical information between the cell and its microenvironment, and necessitates that cells actively maintain a state of homeostasis within a given tissue context. The loss of the ability of tumour cells to establish correct adhesive interactions with their microenvironment results in disruption of tissue architecture with often fatal consequences for the host organism. This review discusses the role of cell adhesion in the maintenance of tissue structure and analyses how tissue structure regulates epithelial function.

Regulation of Adhesion Strength by Focal Adhesion Position and Cell Shape

2012 ◽  
Author(s):  
Nathan D. Gallant ◽  
Kranthi Kumar Elineni
Keyword(s):  
Cell Adhesion ◽  
Adhesion Strength ◽  
Cell Shape ◽  
Microcontact Printing ◽  
Control Cell ◽  
Focal Adhesions ◽  
Cell Spreading ◽  
Spreading Area ◽  
Hydrodynamic Shear ◽  
Cell Spreading Area

Cell adhesion to extracellular matrices is critical to numerous cellular functions and is primarily mediated by integrin receptors. Binding and aggregation of integrins leads to the formation of focal adhesions (FA) which connect the cytoskeleton to the extracellular matrix in order to reinforce adhesion and transmit signals [1]. Preliminary observations indicated preferential recruitment of FAs to the periphery of the cell spreading area on both uniformly coated and micropatterned fibronectin surfaces (Fig. 1). The current study investigates the biophysical regulation of cell adhesion strength based on the size and position of FA with the central hypothesis that peripheral FAs stabilize adhesion strength. The hypothesis was tested by delineating the cell spreading area from the total cell adhesive area by employing microcontact printing to pattern substrates with a series of circular and annular adhesive islands which control cell shape (Fig. 2). A well characterized hydrodynamic shear assay known as the spinning disk device was used to quantify the adhesion strength of cells adhered to the micropatterns [2].

scholarly journals Enlazin, a Natural Fusion of Two Classes of Canonical Cytoskeletal Proteins, Contributes to Cytokinesis Dynamics

2006 ◽  
Vol 17 (12) ◽  
pp. 5275-5286 ◽  
Author(s):  
Edelyn Octtaviani ◽  
Janet C. Effler ◽  
Douglas N. Robinson
Keyword(s):  
Cell Adhesion ◽  
Cell Mechanics ◽  
Cell Shape ◽  
Cytoskeletal Proteins ◽  
Dominant Negative ◽  
Cortical Tension ◽  
Associated Proteins ◽  
Shape Changes ◽  
Novel Protein

Cytokinesis requires a complex network of equatorial and global proteins to regulate cell shape changes. Here, using interaction genetics, we report the first characterization of a novel protein, enlazin. Enlazin is a natural fusion of two canonical classes of actin-associated proteins, the ezrin-radixin-moesin family and fimbrin, and it is localized to actin-rich structures. A fragment of enlazin, enl-tr, was isolated as a genetic suppressor of the cytokinesis defect of cortexillin-I mutants. Expression of enl-tr disrupts expression of endogenous enlazin, indicating that enl-tr functions as a dominant-negative lesion. Enlazin is distributed globally during cytokinesis and is required for cortical tension and cell adhesion. Consistent with a role in cell mechanics, inhibition of enlazin in a cortexillin-I background restores cytokinesis furrowing dynamics and suppresses the growth-in-suspension defect. However, as expected for a role in cell adhesion, inhibiting enlazin in a myosin-II background induces a synthetic cytokinesis phenotype, frequently arresting furrow ingression at the dumbbell shape and/or causing recession of the furrow. Thus, enlazin has roles in cell mechanics and adhesion, and these roles seem to be differentially significant for cytokinesis, depending on the genetic background.

Sign in / Sign up

Export Citation Format

Share Document