Focal Adhesion Proteins Regulate Cell–Matrix and Cell–Cell Adhesion and Act as Force Sensors

2020 ◽  
pp. 95-140
Author(s):  
Claudia Tanja Mierke
Keyword(s):  
Cell Adhesion ◽  
Focal Adhesion ◽  
Force Sensors ◽  
Adhesion Proteins ◽  
Cell Matrix ◽  
Focal Adhesion Proteins ◽  
Cell Cell

scholarly journals Diverse cell junctions with unique molecular composition in tissues of a sponge (Porifera)

EvoDevo ◽  
2019 ◽  
Vol 10 (1) ◽  
Author(s):  
Jennyfer M. Mitchell ◽  
Scott A. Nichols
Keyword(s):  
Extracellular Matrix ◽  
Focal Adhesion ◽  
Adherens Junction ◽  
Focal Adhesions ◽  
Molecular Composition ◽  
Cell Junctions ◽  
Adhesion Proteins ◽  
Focal Adhesion Proteins ◽  
Junction Protein ◽  
Cell Cell

Abstract The integrity and organization of animal tissues depend upon specialized protein complexes that mediate adhesion between cells with each other (cadherin-based adherens junctions), and with the extracellular matrix (integrin-based focal adhesions). Reconstructing how and when these cell junctions evolved is central to understanding early tissue evolution in animals. We examined focal adhesion protein homologs in tissues of the freshwater sponge, Ephydatia muelleri (phylum Porifera; class Demospongiae). Our principal findings are that (1) sponge focal adhesion homologs (integrin, talin, focal adhesion kinase, etc.) co-precipitate as a complex, separate from adherens junction proteins; (2) that actin-based structures resembling focal adhesions form at the cell–substrate interface, and their abundance is dynamically regulated in response to fluid shear; (3) focal adhesion proteins localize to both cell–cell and cell–extracellular matrix adhesions, and; (4) the adherens junction protein β-catenin is co-distributed with focal adhesion proteins at cell–cell junctions everywhere except the choanoderm, and at novel junctions between cells with spicules, and between cells with environmental bacteria. These results clarify the diversity, distribution and molecular composition of cell junctions in tissues of E. muelleri, but raise new questions about their functional properties and ancestry.

scholarly journals Activity and Distribution of Paxillin, Focal Adhesion Kinase, and Cadherin Indicate Cooperative Roles during Zebrafish Morphogenesis

2003 ◽  
Vol 14 (8) ◽  
pp. 3065-3081 ◽  
Author(s):  
Bryan D. Crawford ◽  
Clarissa A. Henry ◽  
Todd A. Clason ◽  
Amanda L. Becker ◽  
Merrill B. Hille
Keyword(s):  
Cell Adhesion ◽  
Focal Adhesion Kinase ◽  
Focal Adhesion ◽  
Adhesion Protein ◽  
Focal Adhesion Proteins ◽  
Somite Formation ◽  
Epithelial Junctions ◽  
Notochord Cells ◽  
Danio Rerio Embryos ◽  
Cell Cell

We investigated the focal adhesion proteins paxillin and Fak, and the cell-cell adhesion protein cadherin in developing zebrafish (Danio rerio) embryos. Cadherins are expressed in presomitic mesoderm where they delineate cells. The initiation of somite formation coincides with an increase in the phosphorylation of Fak, and the accumulation of Fak, phosphorylated Fak, paxillin, and fibronectin at nascent somite boundaries. In the notochord, cadherins are expressed on cells during intercalation, and phosphorylated Fak accumulates in circumferential rings where the notochord cells contact laminin in the perichordal sheath. Subsequently, changes in the orientations of collagen fibers in the sheath suggest that Fak-mediated adhesion allows longitudinal expansion of the notochord, but not lateral expansion, resulting in notochord elongation. Novel observations showed that focal adhesion kinase and paxillin concentrate at sites of cell-cell adhesion in the epithelial enveloping layer and may associate with actin cytoskeleton at epithelial junctions containing cadherins. Fak is phosphorylated at these epithelial junctions but is not phosphorylated on Tyr397, implicating a noncanonical mechanism of regulation. These data suggest that Fak and paxillin may function in the integration of cadherin-based and integrin-based cell adhesion during the morphogenesis of the early zebrafish embryo.

Regulation of reactive oxygen species-induced endothelial cell-cell and cell-matrix contacts by focal adhesion kinase and adherens junction proteins

2005 ◽  
Vol 289 (6) ◽  
pp. L999-L1010 ◽  
Author(s):  
Peter V. Usatyuk ◽  
Viswanathan Natarajan
Keyword(s):  
Cell Adhesion ◽  
Focal Adhesion Kinase ◽  
Tyrosine Phosphorylation ◽  
Focal Adhesion ◽  
Barrier Function ◽  
Fiber Formation ◽  
Actin Stress Fiber ◽  
Cell Matrix ◽  
Cell Cell

Oxidants, generated by activated neutrophils, have been implicated in the pathophysiology of vascular disorders and lung injury; however, mechanisms of oxidant-mediated endothelial barrier dysfunction are unclear. Here, we have investigated the role of focal adhesion kinase (FAK) in regulating hydrogen peroxide (H2O2)-mediated tyrosine phosphorylation of intercellular adhesion proteins and barrier function in endothelium. Treatment of bovine pulmonary artery endothelial cells (BPAECs) with H2O2 increased tyrosine phosphorylation of FAK, paxillin, β-catenin, and vascular endothelial (VE)-cadherin and decreased transendothelial electrical resistance (TER), an index of cell-cell adhesion and/or cell-matrix adhesion. To study the role of FAK in H2O2-induced TER changes, BPAECs were transfected with vector or FAK wild-type or FAK-related non-kinase (FRNK) plasmids. Overexpression of FRNK reduced FAK expression and attenuated H2O2-mediated tyrosine phosphorylation of FAK, paxillin, β-catenin, and VE-cadherin and cell-cell adhesion. Additionally, FRNK prevented H2O2-induced distribution of FAK, paxillin, β-catenin, or VE-cadherin toward focal adhesions and cell-cell adhesions but not actin stress fiber formation. These results suggest that activation of FAK by H2O2 is an important event in oxidant-mediated VE barrier function regulated by cell-cell and cell-matrix contacts.

Effect of Focal Adhesion Proteins on Endothelial Cell Adhesion, Motility and Orientation Response to Cyclic Strain

2009 ◽  
Vol 38 (1) ◽  
pp. 208-222 ◽  
Author(s):  
Hai Ngu ◽  
Yunfeng Feng ◽  
Lan Lu ◽  
Sara J. Oswald ◽  
Gregory D. Longmore ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Endothelial Cell ◽  
Focal Adhesion ◽  
Cyclic Strain ◽  
Adhesion Proteins ◽  
Focal Adhesion Proteins ◽  
Orientation Response ◽  
Endothelial Cell Adhesion

scholarly journals CAIR-1/BAG-3 modulates cell adhesion and migration by downregulating activity of focal adhesion proteins

2006 ◽  
Vol 312 (15) ◽  
pp. 2962-2971 ◽  
Author(s):  
Jareer N. Kassis ◽  
Elizabeth A. Guancial ◽  
Howard Doong ◽  
Victoria Virador ◽  
Elise C. Kohn
Keyword(s):  
Cell Adhesion ◽  
Focal Adhesion ◽  
Adhesion Proteins ◽  
Focal Adhesion Proteins ◽  
Cell Adhesion And Migration ◽  
And Migration

Epithelial Morphogenesis Driven by Cell-Matrix vs. Cell-Cell Adhesion

2020 ◽  
Author(s):  
Shaohe Wang ◽  
Kazue Matsumoto ◽  
Kenneth M. Yamada
Keyword(s):  
Cell Adhesion ◽  
Epithelial Morphogenesis ◽  
Cell Matrix ◽  
Cell Cell

scholarly journals SPEG binds with desmin and its deficiency causes defects in triad and focal adhesion proteins

2020 ◽  
Author(s):  
Shiyu Luo ◽  
Qifei Li ◽  
Jasmine Lin ◽  
Quinn Murphy ◽  
Isabelle Marty ◽  
...  
Keyword(s):  
Focal Adhesion ◽  
Skeletal Muscles ◽  
Striated Muscle ◽  
Calcium Handling ◽  
Intermediate Filament Protein ◽  
Β1 Integrin ◽  
Adhesion Proteins ◽  
Focal Adhesion Proteins ◽  
Early Endosomes

Abstract SPEG, a member of the myosin light chain kinase family, is localized at the level of triad surrounding myofibrils in skeletal muscles. In humans, SPEG mutations are associated with centronuclear myopathy and cardiomyopathy. Using a striated muscle specific Speg-knockout (KO) mouse model, we have previously shown that SPEG is critical for triad maintenance and calcium handling. Here we further examined the molecular function of SPEG and characterized the effects of SPEG deficiency on triad and focal adhesion proteins. We used yeast two-hybrid assay, and identified desmin, an intermediate filament protein, to interact with SPEG and confirmed this interaction by co-immunoprecipitation. Using domain-mapping assay, we defined that Ig-like and fibronectin III domains of SPEG interact with rod domain of desmin. In skeletal muscles, SPEG depletion leads to desmin aggregates in vivo and a shift in desmin equilibrium from soluble to insoluble fraction. We also profiled the expression and localization of triadic proteins in Speg-KO mice using western blot and immunofluorescence. The amounts of RyR1 and triadin were markedly reduced, whereas DHPRα1, SERCA1, and triadin were abnormally accumulated in discrete areas of Speg-KO myofibers. In addition, Speg-KO muscles exhibited internalized vinculin and β1 integrin, both of which are critical components of the focal adhesion complex. Further, β1 integrin was abnormally accumulated in early endosomes of Speg-KO myofibers. These results demonstrate that SPEG-deficient skeletal muscles exhibit several pathological features similar to those seen in MTM1 deficiency. Defects of shared cellular pathways may underlie these structural and functional abnormalities in both types of diseases.

The Kindlin protein family: new members to the club of focal adhesion proteins

2009 ◽  
Vol 19 (10) ◽  
pp. 504-513 ◽  
Author(s):  
Alexander Meves ◽  
Christopher Stremmel ◽  
Kay Gottschalk ◽  
Reinhard Fässler
Keyword(s):  
Focal Adhesion ◽  
Protein Family ◽  
New Members ◽  
Adhesion Proteins ◽  
Focal Adhesion Proteins
Sign in / Sign up

Export Citation Format

Share Document