scholarly journals The focal adhesion-associated proteins DOCK5 and GIT2 comprise a rheostat in control of epithelial invasion

Oncogene ◽  
2016 ◽  
Vol 36 (13) ◽  
pp. 1816-1828 ◽  
Author(s):  
S R Frank ◽  
C P Köllmann ◽  
J F van Lidth de Jeude ◽  
J R Thiagarajah ◽  
L H Engelholm ◽  
...  
Keyword(s):  
Focal Adhesion ◽  
Associated Proteins ◽  
Epithelial Invasion

Change in distribution of cytoskeleton-associated proteins, lasp-1 and palladin, during uterine receptivity in the rat endometrium

2018 ◽  
Vol 30 (11) ◽  
pp. 1482 ◽  
Author(s):  
Leigh Nicholson ◽  
Laura Lindsay ◽  
Christopher R. Murphy
Keyword(s):  
Plasma Membrane ◽  
Focal Adhesion ◽  
Early Pregnancy ◽  
Morphological Changes ◽  
Cytoskeletal Proteins ◽  
Initial Contact ◽  
Luminal Epithelium ◽  
Uterine Receptivity ◽  
Uterine Lumen ◽  
Associated Proteins

The epithelium of the uterine lumen is the first point of contact with the blastocyst before implantation. To facilitate pregnancy, these uterine epithelial cells (UECs) undergo morphological changes specific to the receptive uterus. These changes include basal, lateral and apical alterations in the plasma membrane of UECs. This study looked at the cytoskeletal and focal adhesion-associated proteins, lasp-1 and palladin, in the uterus during early pregnancy in the rat. Two palladin isoforms, 140 kDa and 90 kDa, were analysed, with the migration-associated 140-kDa isoform increasing significantly at the time of implantation when compared with the time of fertilisation. Lasp-1 was similarly increased at this time, whilst also being located predominantly apically and laterally in the UECs, suggesting a role in the initial contact between the UECs and the blastocyst. This is the first study to investigate palladin and lasp-1 in the uterine luminal epithelium and suggests an importance for these cytoskeletal proteins in the morphological changes the UECs undergo for pregnancy to occur.

scholarly journals Tyrosine phosphorylation and cytoskeletal tension regulate the release of fibroblast adhesions.

1995 ◽  
Vol 131 (2) ◽  
pp. 525-537 ◽  
Author(s):  
E Crowley ◽  
A F Horwitz
Keyword(s):  
Tyrosine Phosphorylation ◽  
Focal Adhesion ◽  
Okadaic Acid ◽  
Tyrosine Phosphatase ◽  
Focal Adhesions ◽  
Cell System ◽  
Cell Contraction ◽  
Permeabilized Cell ◽  
Variable Intensity ◽  
Associated Proteins

We have investigated the mechanisms by which fibroblasts release their adhesions to the extracellular matrix substrata using a permeabilized cell system in which the adhesions remain relatively stable. A large number of different molecules were assayed for their effect on focal adhesion stability using immunofluorescence with antibodies against different focal adhesion constituents. ATP uniquely stimulates a rapid breakdown of focal adhesions, and at high ATP concentrations (> 5 mM), many cells are released from the dish. The remaining cells appear contracted with talin, alpha-actinin, and vinculin localized diffusely throughout the cell. Integrin containing tracks of variable intensity outline the regions where cells had resided before they detached from the substratum. At lower ATP concentrations (0.5-5 mM) the cells remain spread; however the focal adhesion components, including integrin, show an array of phenotypes ranging from diffusely localized throughout the cell to a localization in small, thin focal adhesions. Okadaic acid, a serine, threonine phosphatase inhibitor, enhances the contracted phenotype, even at low concentrations (0.5 mM) of ATP. The localization of focal adhesion components is different in okadaic acid-treated cells. In highly contracted cells, integrin is present in tracks where the cells resided before the contraction; however focal adhesions are no longer apparent. Talin, vinculin, and alpha-actinin localize in trabecular networks toward the periphery of the cell. Interestingly, phosphotyrosine staining as well as nascent, intracellular integrin precedes the recruitment of focal adhesion constituents into the trabecular network. The ATP-stimulated focal adhesion breakdown appears to operate through two mechanisms. First, ATP stimulates the tyrosine phosphorylation of several cytoskeletally associated proteins. These tyrosine phosphorylations correlated well with focal adhesion breakdown. Furthermore, addition of a recombinant, constitutively active tyrosine phosphatase inhibits both the tyrosine phosphorylations and the breakdown of the focal adhesions. None of the major tyrosine phosphoproteins are FAK, integrin, tensin, paxillin, or other phosphoproteins implicated in focal adhesion assembly. The second mechanism is cell contraction. High ATP concentrations, or lower ATP concentrations in the presence of okadaic acid induce cell contraction. Inhibiting the contraction by addition of a heptapeptide IRICRKG, which blocks the actin-myosin interaction, also inhibits focal adhesion breakdown. Neither the peptide nor the phosphatase inhibits focal adhesion breakdown under all conditions suggesting that both tension and tyrosine phosphorylations mediate the release of adhesions.

Focal adhesion kinase and associated proteins

1994 ◽  
Vol 6 (5) ◽  
pp. 705-710 ◽  
Author(s):  
Michael D. Schaller ◽  
J. Thomas Parsons
Keyword(s):  
Focal Adhesion Kinase ◽  
Focal Adhesion ◽  
Associated Proteins

scholarly journals Novel functions for integrin-associated proteins revealed by myofibril attachment in Drosophila

2018 ◽  
Author(s):  
Hannah J. Green ◽  
Annabel G. M. Griffiths ◽  
Nicholas H. Brown
Keyword(s):  
Focal Adhesion Kinase ◽  
Focal Adhesion ◽  
Genetic Interactions ◽  
Molecular Composition ◽  
Myotendinous Junction ◽  
Membrane Anchor ◽  
Associated Proteins ◽  
Flight Muscles ◽  
Complex Architecture

AbstractWe use the myotendinous junction of Drosophila flight muscles to explore why many integrin associated proteins (IAPs) are needed and how their function is coordinated. These muscles revealed new functions for IAPs not required for viability: Focal Adhesion Kinase (FAK), RSU1, tensin and vinculin. Genetic interactions demonstrated a balance between positive and negative activities, with vinculin and tensin positively regulating adhesion, while FAK inhibits elevation of integrin activity by tensin, and RSU1 keeps PINCH activity in check. The molecular composition of myofibril termini resolves into 4 distinct layers, one of which is built by a mechanotransduction cascade: vinculin facilitates mechanical opening of filamin, which works with the Arp2/3 activator WASH to build an actin-rich layer positioned between integrins and the first sarcomere. Thus, integration of IAP activity is needed to build the complex architecture of the myotendinous junction, linking the membrane anchor to the sarcomere.Graphical abstract

scholarly journals Expression levels of the focal adhesion-associated proteins paxillin and p130CAS in canine and feline mammary tumors

2003 ◽  
Vol 34 (2) ◽  
pp. 193-202 ◽  
Author(s):  
Antonio Scibelli ◽  
Danila d'Angelo ◽  
Alessandra Pelagalli ◽  
Simona Tafuri ◽  
Luigi Avallone ◽  
...  
Keyword(s):  
Focal Adhesion ◽  
Mammary Tumors ◽  
Expression Levels ◽  
Associated Proteins
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