Characterization of focal adhesion assembly in XR1 glial cells

Folsom, Timothy D.; Sakaguchi, Donald S.

doi:10.1002/(sici)1098-1136(199708)20:4<348::aid-glia7>3.0.co;2-1

Cited by 12 publications

(3 citation statements)

References 61 publications

(95 reference statements)

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“…The majority of work regarding effects of tyrosine phosphorylation utilized cells commencing spreading or recovering from starvation. A few reports that used well spread nonstarved cells focused on stability and phosphorylation status of focal adhesions and suggest that inhibitors of tyrosine kinases and phosphatases affect most effectively adhesions in statu nascendi, whereas mature adhesions are either less sensitive or insensitive to those inhibitors (41)(42)(43)(44). Here we show that well spread, nonstarved L fibroblasts treated with inhibitors of tyrosine kinases and phosphatases undergo dramatic changes in shape and degree of spreading.…”

Section: Discussionsupporting

confidence: 48%

Calreticulin Affects β-Catenin-associated Pathways

Fadel

Szewczenko-Pawlikowski

Leclerc

et al. 2001

Journal of Biological Chemistry

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Calreticulin, a Ca2؉ storage protein and chaperone in the endoplasmic reticulum, also modulates cell adhesiveness. Overexpression of calreticulin correlates with (i) increased cell adhesiveness, (ii) increased expression of N-cadherin and vinculin, and (iii) decreased protein phosphorylation on tyrosine. Among proteins that are dephosphorylated in cells that overexpress calreticulin is ␤-catenin, a structural component of cadherindependent adhesion complexes, a member of the armadillo family of proteins and a part of the Wnt signaling pathway. We postulate that the changes in cell adhesiveness may be due to calreticulin-mediated effects on a signaling pathway from the endoplasmic reticulum, which impinges on the Wnt signaling pathway via the cadherin/catenin protein system and involves changes in the activity of protein-tyrosine kinases and/or phosphatases. The endoplasmic reticulum (ER)1 plays a critical role in the synthesis and chaperoning of membrane-associated proteins and secreted proteins (1). It is also an important site for the storage and release of Ca 2ϩ (2). In fact, the ER is the major signal transducing organelle within the cell, continuously responding to extracellular stimuli by releasing Ca 2ϩ (3,4). The ER is also sensitive to intracellular signaling; in response to a variety of stimuli signals are transduced from the ER to the cytoplasm, the plasma membrane, and the nucleus, and they affect a variety of cellular activities including Ca 2ϩ influx, protein folding, and synthesis, cholesterol synthesis, and transcription (5-8). Signaling from the extracellular space to the cell interior has long been the subject of intense research. In contrast, little is known about intracellular signaling from the ER. The lumen of the ER is a unique environment, which contains a high concentration of Ca 2ϩ -binding chaperones (2). Calreticulin, a major Ca 2ϩ -binding protein resident in the ER, is ubiquitous in eukaryotic cells (9). It functions as a molecular chaperone (10, 11) and also participates in ER-dependent Ca 2ϩ homeostasis (2, 9). Calreticulin also affects processes external to the ER, such as steroid-sensitive gene expression and cell adhesiveness (12). Although the Ca 2ϩ storage and chaperone functions of calreticulin are consistent with its localization to the lumen of the ER and with its structure, it is not obvious how it can affect cell adhesiveness at the level of the plasma membrane. To investigate the mechanisms behind calreticulindependent modulation of cell adhesiveness, we used well characterized mouse L fibroblasts differentially expressing calreticulin (13-15). Here we show that stable overexpression of fulllength, ER-targeted calreticulin correlates with an increased adhesiveness in transformed fibroblasts, such that their cohesion resembles that of epithelial cells in culture. We also show that changes in the expression of calreticulin affect the tyrosine phosphorylation of cellular proteins, including ␤-catenin. ␤-Catenin is a structural component of cadherin-mediated adhesion comple...

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Section: Discussionsupporting

confidence: 48%

Calreticulin Affects β-Catenin-associated Pathways

Fadel

Szewczenko-Pawlikowski

Leclerc

et al. 2001

Journal of Biological Chemistry

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“…In Xenopus XR1 glial cells, derived from retinal neuroepithelium, was shown colocalization of myosin heavy chain-A with filamentous (F)-actin microfilament, vinculin, and β 1 integrin at FA sites. Colocalization of these proteins supported their contribution to the assembly of the adhesion process (61,62). Cell adhesion is one of the essential steps in cell motility (for review see 63; 64).…”

Section: Discussionmentioning

confidence: 97%

“…Transforming growth factor, cellular FN splice variant ED-A FN, and increased matrix stress induce α-SMA expression and formation of differentiated myofibroblasts which are characterized by the development of supermature FAs containing α-SMA in stress fibers, high vinculin expression intracellularly, and ED-A FN in the extracellular space (31,32). So, cytoskeletal elements seem to have functional roles in the assembly of cell adhesions (5,33,34), and adhesive interactions are believed to play important roles in directing the migration, proliferation, and differentiation of cells (6).…”

Section: Discussionmentioning

confidence: 99%

Expression of Proteins Associated with Cell-Matrix Adhesion in Proliferative Vitreoretinopathy Designed by Dispase Model

Işıksoy

Başmak

Dündar

et al. 2007

European Journal of Ophthalmology

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Vinculin seems to be involved in PVR pathogenesis. Variability in co-distribution of the expression of vinculin, FN, and alfa-SMA reflects the dynamic interactions evolving between cell and extracellular matrix during the epi- and subretinal membrane formations. The results of this study were determined not to be in support of the assumption that CD44 has a functional role in the pathogenesis of PVR.

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Disruption of actin-myosin interactions results in the inhibition of focal adhesion assembly inXenopus XR1 glial cells

Folsom¹,

Sakaguchi²

1999

Glia

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Characterization of focal adhesion assembly in XR1 glial cells

Cited by 12 publications

References 61 publications

Calreticulin Affects β-Catenin-associated Pathways

Calreticulin Affects β-Catenin-associated Pathways

Expression of Proteins Associated with Cell-Matrix Adhesion in Proliferative Vitreoretinopathy Designed by Dispase Model

Disruption of actin-myosin interactions results in the inhibition of focal adhesion assembly inXenopus XR1 glial cells

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