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Journal articles on the topic 'Adhesion Complex'

Author: Grafiati

Published: 4 June 2021

Last updated: 7 February 2022

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1

Young, Katherine A., Laura Biggins, and Hayley J. Sharpe. "Protein tyrosine phosphatases in cell adhesion." Biochemical Journal 478, no. 5 (2021): 1061–83. http://dx.doi.org/10.1042/bcj20200511.

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Adhesive structures between cells and with the surrounding matrix are essential for the development of multicellular organisms. In addition to providing mechanical integrity, they are key signalling centres providing feedback on the extracellular environment to the cell interior, and vice versa. During development, mitosis and repair, cell adhesions must undergo extensive remodelling. Post-translational modifications of proteins within these complexes serve as switches for activity. Tyrosine phosphorylation is an important modification in cell adhesion that is dynamically regulated by the prot

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2

Sebé-Pedrós, Arnau, and Iñaki Ruiz-Trillo. "Integrin-mediated adhesion complex." Communicative & Integrative Biology 3, no. 5 (2010): 475–77. http://dx.doi.org/10.4161/cib.3.5.12603.

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Mistry, Shiv A., Avi M. Desai, Peidong He, et al. "In vitro investigation of chitosan-polygalacturonic acid polyelectrolyte complex (PEC) biomaterials as anti-adhesive substrates for preventing adhesion formation." TECHNOLOGY 06, no. 03n04 (2018): 110–17. http://dx.doi.org/10.1142/s2339547818500073.

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Adhesions are an abnormal union of membranous surfaces. They are a painful and expensive consequence of abdominal surgeries, specifically in the peritoneal cavity. This complication requires a second surgery to remove the problem, known as adhesiolysis, which we are trying to avoid. Current solutions to adhesion formation either lack efficacy or induce an inflammatory response in the peritoneum. Our focus is to develop a post-surgical adhesion prevention polyelectrolyte complex (PEC) film, composed of an optimal ratio of chitosan (Chi) and polygalacturonic acid (PgA) to prevent adhesion format

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Bach, Cuc T. T., Sarah Creed, Jessie Zhong, et al. "Tropomyosin Isoform Expression Regulates the Transition of Adhesions To Determine Cell Speed and Direction." Molecular and Cellular Biology 29, no. 6 (2009): 1506–14. http://dx.doi.org/10.1128/mcb.00857-08.

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ABSTRACT The balance of transition between distinct adhesion types contributes to the regulation of mesenchymal cell migration, and the characteristic association of adhesions with actin filaments led us to question the role of actin filament-associating proteins in the transition between adhesive states. Tropomyosin isoform association with actin filaments imparts distinct filament structures, and we have thus investigated the role for tropomyosins in determining the formation of distinct adhesion structures. Using combinations of overexpression, knockdown, and knockout approaches, we establi

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Katrín Hákonardóttir, Guðlaug, Pablo López-Ceballos, Alejandra Donají Herrera-Reyes, Raibatak Das, Daniel Coombs, and Guy Tanentzapf. "In vivo quantitative analysis of Talin turnover in response to force." Molecular Biology of the Cell 26, no. 22 (2015): 4149–62. http://dx.doi.org/10.1091/mbc.e15-05-0304.

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Cell adhesion to the extracellular matrix (ECM) allows cells to form and maintain three-dimensional tissue architecture. Cell–ECM adhesions are stabilized upon exposure to mechanical force. In this study, we used quantitative imaging and mathematical modeling to gain mechanistic insight into how integrin-based adhesions respond to increased and decreased mechanical forces. A critical means of regulating integrin-based adhesion is provided by modulating the turnover of integrin and its adhesion complex (integrin adhesion complex [IAC]). The turnover of the IAC component Talin, a known mechanose

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Lotz, M. M., C. A. Burdsal, H. P. Erickson, and D. R. McClay. "Cell adhesion to fibronectin and tenascin: quantitative measurements of initial binding and subsequent strengthening response." Journal of Cell Biology 109, no. 4 (1989): 1795–805. http://dx.doi.org/10.1083/jcb.109.4.1795.

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Cell-substratum adhesion strengths have been quantified using fibroblasts and glioma cells binding to two extracellular matrix proteins, fibronectin and tenascin. A centrifugal force-based adhesion assay was used for the adhesive strength measurements, and the corresponding morphology of the adhesions was visualized by interference reflection microscopy. The initial adhesions as measured at 4 degrees C were on the order of 10(-5)dynes/cell and did not involve the cytoskeleton. Adhesion to fibronectin after 15 min at 37 degrees C were more than an order of magnitude stronger; the strengthening

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7

Greenwood, Jeffrey A., Anne B. Theibert, Glenn D. Prestwich, and Joanne E. Murphy-Ullrich. "Restructuring of Focal Adhesion Plaques by Pi 3-Kinase." Journal of Cell Biology 150, no. 3 (2000): 627–42. http://dx.doi.org/10.1083/jcb.150.3.627.

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Focal adhesions are an elaborate network of interconnecting proteins linking actin stress fibers to the extracellular matrix substrate. Modulation of the focal adhesion plaque provides a mechanism for the regulation of cellular adhesive strength. Using interference reflection microscopy, we found that activation of phosphoinositide 3-kinase (PI 3-kinase) by PDGF induces the dissipation of focal adhesions. Loss of this close apposition between the cell membrane and the extracellular matrix coincided with a redistribution of α-actinin and vinculin from the focal adhesion complex to the Triton X-

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8

Israeli, Sharon, Kurt Amsler, Nadezhda Zheleznova, and Patricia D. Wilson. "Abnormalities in focal adhesion complex formation, regulation, and function in human autosomal recessive polycystic kidney disease epithelial cells." American Journal of Physiology-Cell Physiology 298, no. 4 (2010): C831—C846. http://dx.doi.org/10.1152/ajpcell.00032.2009.

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Integrin-associated focal adhesion complex formation and turnover plays an essential role in directing interactions between epithelial cells and the extracellular matrix during organogenesis, leading to appropriate cell spreading, cell-matrix adhesion, and migration. Autosomal recessive polycystic kidney disease (ARPKD) is associated with loss of function of PKHD1-encoded protein fibrocystin-1 and is characterized by cystic dilation of renal collecting tubules (CT) in utero and loss of renal function in patients if they survive the perinatal period. Normal polycystin-1 (PC-1)/focal adhesion co

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Westhoff, M. A., B. Serrels, V. J. Fincham, M. C. Frame, and N. O. Carragher. "Src-Mediated Phosphorylation of Focal Adhesion Kinase Couples Actin and Adhesion Dynamics to Survival Signaling." Molecular and Cellular Biology 24, no. 18 (2004): 8113–33. http://dx.doi.org/10.1128/mcb.24.18.8113-8133.2004.

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ABSTRACT Integrin-associated focal adhesions not only provide adhesive links between cellular actin and extracellular matrix but also are sites of signal transmission into the cell interior. Many cell responses signal through focal adhesion kinase (FAK), often by integrin-induced autophosphorylation of FAK or phosphorylation by Src family kinases. Here, we used an interfering FAK mutant (4-9F-FAK) to show that Src-dependent FAK phosphorylation is required for focal adhesion turnover and cell migration, by controlling assembly of a calpain 2/FAK/Src/p42ERK complex, calpain activation, and prote

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González-Tarragó, Víctor, Alberto Elosegui-Artola, Elsa Bazellières, Roger Oria, Carlos Pérez-González та Pere Roca-Cusachs. "Binding of ZO-1 to α5β1 integrins regulates the mechanical properties of α5β1–fibronectin links". Molecular Biology of the Cell 28, № 14 (2017): 1847–52. http://dx.doi.org/10.1091/mbc.e17-01-0006.

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Fundamental processes in cell adhesion, motility, and rigidity adaptation are regulated by integrin-mediated adhesion to the extracellular matrix (ECM). The link between the ECM component fibronectin (fn) and integrin α5β1 forms a complex with ZO-1 in cells at the edge of migrating monolayers, regulating cell migration. However, how this complex affects the α5β1-fn link is unknown. Here we show that the α5β1/ZO-1 complex decreases the resistance to force of α5β1–fn adhesions located at the edge of migrating cell monolayers while also increasing α5β1 recruitment. Consistently with a molecular c

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11

MATSUBA, Go. "Crystallization of Stereo Complex of Poly（ lactic acid）." Journal of The Adhesion Society of Japan 54, no. 12 (2018): 444–50. http://dx.doi.org/10.11618/adhesion.54.444.

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12

Kim, Hyo Jeong, Byeongseon Yang, Tae Yoon Park, Seonghye Lim, and Hyung Joon Cha. "Complex coacervates based on recombinant mussel adhesive proteins: their characterization and applications." Soft Matter 13, no. 42 (2017): 7704–16. http://dx.doi.org/10.1039/c7sm01735a.

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13

Stewart, Rachel M., Amanda E. Zubek, Kathryn A. Rosowski, Sarah M. Schreiner, Valerie Horsley, and Megan C. King. "Nuclear–cytoskeletal linkages facilitate cross talk between the nucleus and intercellular adhesions." Journal of Cell Biology 209, no. 3 (2015): 403–18. http://dx.doi.org/10.1083/jcb.201502024.

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The linker of nucleoskeleton and cytoskeleton (LINC) complex allows cells to actively control nuclear position by coupling the nucleus to the cytoplasmic cytoskeleton. Nuclear position responds to the formation of intercellular adhesions through coordination with the cytoskeleton, but it is not known whether this response impacts adhesion function. In this paper, we demonstrate that the LINC complex component SUN2 contributes to the mechanical integrity of intercellular adhesions between mammalian epidermal keratinocytes. Mice deficient for Sun2 exhibited irregular hair follicle intercellular

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Emond, Michelle R., Sayantanee Biswas, Cheasequah J. Blevins, and James D. Jontes. "A complex of Protocadherin-19 and N-cadherin mediates a novel mechanism of cell adhesion." Journal of Cell Biology 195, no. 7 (2011): 1115–21. http://dx.doi.org/10.1083/jcb.201108115.

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During embryonic morphogenesis, adhesion molecules are required for selective cell–cell interactions. The classical cadherins mediate homophilic calcium-dependent cell adhesion and are founding members of the large and diverse cadherin superfamily. The protocadherins are the largest subgroup within this superfamily, yet their participation in calcium-dependent cell adhesion is uncertain. In this paper, we demonstrate a novel mechanism of adhesion, mediated by a complex of Protocadherin-19 (Pcdh19) and N-cadherin (Ncad). Although Pcdh19 alone is only weakly adhesive, the Pcdh19–Ncad complex exh

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15

Gallant, Nathan D., Kristin E. Michael, and Andrés J. García. "Cell Adhesion Strengthening: Contributions of Adhesive Area, Integrin Binding, and Focal Adhesion Assembly." Molecular Biology of the Cell 16, no. 9 (2005): 4329–40. http://dx.doi.org/10.1091/mbc.e05-02-0170.

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Mechanical interactions between a cell and its environment regulate migration, contractility, gene expression, and cell fate. We integrated micropatterned substrates to engineer adhesive area and a hydrodynamic assay to analyze fibroblast adhesion strengthening on fibronectin. Independently of cell spreading, integrin binding and focal adhesion assembly resulted in rapid sevenfold increases in adhesion strength to steady-state levels. Adhesive area strongly modulated adhesion strength, integrin binding, and vinculin and talin recruitment, exhibiting linear increases for small areas. However, a

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Toret, Christopher P., Caitlin Collins, and W. James Nelson. "An Elmo–Dock complex locally controls Rho GTPases and actin remodeling during cadherin-mediated adhesion." Journal of Cell Biology 207, no. 5 (2014): 577–87. http://dx.doi.org/10.1083/jcb.201406135.

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Cell–cell contact formation is a dynamic process requiring the coordination of cadherin-based cell–cell adhesion and integrin-based cell migration. A genome-wide RNA interference screen for proteins required specifically for cadherin-dependent cell–cell adhesion identified an Elmo–Dock complex. This was unexpected as Elmo–Dock complexes act downstream of integrin signaling as Rac guanine-nucleotide exchange factors. In this paper, we show that Elmo2 recruits Dock1 to initial cell–cell contacts in Madin–Darby canine kidney cells. At cell–cell contacts, both Elmo2 and Dock1 are essential for the

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Le Guennec, Loic, Zoé Virion, Haniaa Bouzinba-Ségard, et al. "Receptor recognition by meningococcal type IV pili relies on a specific complex N-glycan." Proceedings of the National Academy of Sciences 117, no. 5 (2020): 2606–12. http://dx.doi.org/10.1073/pnas.1919567117.

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Bacterial infections are frequently based on the binding of lectin-like adhesins to specific glycan determinants exposed on host cell receptors. These interactions confer species-specific recognition and tropism for particular host tissues and represent attractive antibacterial targets. However, the wide structural diversity of carbohydrates hampers the characterization of specific glycan determinants. Here, we characterized the receptor recognition of type IV pili (Tfp), a key adhesive factor present in numerous bacterial pathogens, using Neisseria meningitidis as a model organism. We found t

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Garrod, David, and Tomomi E. Kimura. "Hyper-adhesion: a new concept in cell–cell adhesion." Biochemical Society Transactions 36, no. 2 (2008): 195–201. http://dx.doi.org/10.1042/bst0360195.

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We have developed a new concept of cell–cell adhesion termed ‘hyper-adhesion’, the very strong adhesion adopted by desmosomes. This uniquely desmosomal property accounts for their ability to provide the intercellular links in the desmosome–intermediate filament complex. These links are targeted by diseases, resulting in disruption of the complex with severe consequences. Hyper-adhesion is characteristic of desmosomes in tissues and is believed to result from a highly ordered arrangement of the extracellular domains of the desmosomal cadherins that locks their binding interaction so that it is

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Dompé, Marco, Francisco J. Cedano‐Serrano, Mehdi Vahdati, et al. "Underwater Adhesion of Multiresponsive Complex Coacervates." Advanced Materials Interfaces 7, no. 4 (2019): 1901785. http://dx.doi.org/10.1002/admi.201901785.

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Gupton, Stephanie L., Daisy Riquelme, Shannon K. Hughes-Alford та ін. "Mena binds α5 integrin directly and modulates α5β1 function". Journal of Cell Biology 198, № 4 (2012): 657–76. http://dx.doi.org/10.1083/jcb.201202079.

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Mena is an Ena/VASP family actin regulator with roles in cell migration, chemotaxis, cell–cell adhesion, tumor cell invasion, and metastasis. Although enriched in focal adhesions, Mena has no established function within these structures. We find that Mena forms an adhesion-regulated complex with α5β1 integrin, a fibronectin receptor involved in cell adhesion, motility, fibronectin fibrillogenesis, signaling, and growth factor receptor trafficking. Mena bound directly to the carboxy-terminal portion of the α5 cytoplasmic tail via a 91-residue region containing 13 five-residue “LERER” repeats. I

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Wang, Chau-Zen, Yi-Chun Yeh, and Ming-Jer Tang. "DDR1/E-cadherin complex regulates the activation of DDR1 and cell spreading." American Journal of Physiology-Cell Physiology 297, no. 2 (2009): C419—C429. http://dx.doi.org/10.1152/ajpcell.00101.2009.

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Discoidin domain receptors (DDRs) 1 and 2, collagen receptors, regulate cell adhesion and a broad range of cell behavior. Their adhesion-dependent regulation of signaling associated with adhesion proteins has not been elucidated. We report a novel mechanism: the cross talk of DDR1 and E-cadherin negatively and adhesion dependently regulated both DDR1 activity and DDR1-suppressed cell spreading. E-cadherin forms complexes with both DDR1 isoforms (a and b). E-cadherin regulates DDR1 activity associated with the cell-junction complexes formed between DDR1 and E-cadherin. These complexes are forme

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Tapial Martínez, Paula, Pilar López Navajas, and Daniel Lietha. "FAK Structure and Regulation by Membrane Interactions and Force in Focal Adhesions." Biomolecules 10, no. 2 (2020): 179. http://dx.doi.org/10.3390/biom10020179.

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Focal adhesion kinase (FAK) is a non-receptor tyrosine kinase with key roles in the regulation of cell adhesion migration, proliferation and survival. In cancer FAK is a major driver of invasion and metastasis and its upregulation is associated with poor patient prognosis. FAK is autoinhibited in the cytosol, but activated upon localisation into a protein complex, known as focal adhesion complex. This complex forms upon cell adhesion to the extracellular matrix (ECM) at the cytoplasmic side of the plasma membrane at sites of ECM attachment. FAK is anchored to the complex via multiple sites, in

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Nayal, Anjana, Donna J. Webb, Claire M. Brown, Erik M. Schaefer, Miguel Vicente-Manzanares, and Alan Rick Horwitz. "Paxillin phosphorylation at Ser273 localizes a GIT1–PIX–PAK complex and regulates adhesion and protrusion dynamics." Journal of Cell Biology 173, no. 4 (2006): 587–89. http://dx.doi.org/10.1083/jcb.200509075.

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Continuous adhesion formation and disassembly (adhesion turnover) in the protrusions of migrating cells is regulated by unclear mechanisms. We show that p21-activated kinase (PAK)–induced phosphorylation of serine 273 in paxillin is a critical regulator of this turnover. Paxillin-S273 phosphorylation dramatically increases migration, protrusion, and adhesion turnover by increasing paxillin–GIT1 binding and promoting the localization of a GIT1–PIX–PAK signaling module near the leading edge. Mutants that interfere with the formation of this ternary module abrogate the effects of paxillin-S273 ph

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Levkau, Bodo, Barbara Herren, Hidenori Koyama, Russell Ross, and Elaine W. Raines. "Caspase-mediated Cleavage of Focal Adhesion Kinase pp125FAK and Disassembly of Focal Adhesions in Human Endothelial Cell Apoptosis." Journal of Experimental Medicine 187, no. 4 (1998): 579–86. http://dx.doi.org/10.1084/jem.187.4.579.

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Normal endothelial and epithelial cells undergo apoptosis when cell adhesion and spreading are prevented, implying a requirement for antiapoptotic signals from the extracellular matrix for cell survival. We investigated some of the molecular changes occurring in focal adhesions during growth factor deprivation–induced apoptosis in confluent monolayers of human umbilical vein endothelial cells. Among the first morphologic changes after initiation of the apoptotic process are membrane blebbing, loss of focal adhesion sites, and retraction from the matrix followed by detachment. We observe a spec

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Wang, Shujie, Takashi Watanabe, Kenji Matsuzawa, et al. "Tiam1 interaction with the PAR complex promotes talin-mediated Rac1 activation during polarized cell migration." Journal of Cell Biology 199, no. 2 (2012): 331–45. http://dx.doi.org/10.1083/jcb.201202041.

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Migrating cells acquire front-rear polarity with a leading edge and a trailing tail for directional movement. The Rac exchange factor Tiam1 participates in polarized cell migration with the PAR complex of PAR3, PAR6, and atypical protein kinase C. However, it remains largely unknown how Tiam1 is regulated and contributes to the establishment of polarity in migrating cells. We show here that Tiam1 interacts directly with talin, which binds and activates integrins to mediate their signaling. Tiam1 accumulated at adhesions in a manner dependent on talin and the PAR complex. The interactions of ta

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Dompé, Marco, Francisco Javier Cedano-Serrano, Mehdi Vahdati, et al. "Hybrid Complex Coacervate." Polymers 12, no. 2 (2020): 320. http://dx.doi.org/10.3390/polym12020320.

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Underwater adhesion represents a huge technological challenge as the presence of water compromises the performance of most commercially available adhesives. Inspired by natural organisms, we have designed an adhesive based on complex coacervation, a liquid–liquid phase separation phenomenon. A complex coacervate adhesive is formed by mixing oppositely charged polyelectrolytes bearing pendant thermoresponsive poly(N-isopropylacrylamide) (PNIPAM) chains. The material fully sets underwater due to a change in the environmental conditions, namely temperature and ionic strength. In this work, we inc

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Kim, Y. J. "Modulating the strength of cadherin adhesion: evidence for a novel adhesion complex." Journal of Cell Science 118, no. 17 (2005): 3883–94. http://dx.doi.org/10.1242/jcs.02508.

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Andrews, Robert, Yang Shen, Elizabeth Gardiner, Jing-fei Dong, José López, and Michael Berndt. "The Glycoprotein Ib-IX-V Complex in Platelet Adhesion and Signaling." Thrombosis and Haemostasis 82, no. 08 (1999): 357–64. http://dx.doi.org/10.1055/s-0037-1615854.

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IntroductionThrombosis can result in unstable angina, acute myocardial infarction, or stroke, all major causes of death in the Western world. Circulating platelets become adherent and form an occlusive thrombus, either by exposure to sclerotic lesions following plaque rupture or in response to pathological shear stress in obstructed coronary arteries. This process parallels normal haemostasis, where platelets adhere to the subendothelium at sites of vascular injury, become activated, and recruit additional platelets to the developing thrombus. At high shear, thrombus formation is initiated by

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29

Troyanovsky, Sergey M. "Mechanism of cell–cell adhesion complex assembly." Current Opinion in Cell Biology 11, no. 5 (1999): 561–66. http://dx.doi.org/10.1016/s0955-0674(99)00021-6.

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Pelosi, Marco A., and Marco A. Pelosi. "A New Adhesion Barrier for Complex Myomectomy." Obstetrics & Gynecology 99, Supplement (2002): 33S. http://dx.doi.org/10.1097/00006250-200204001-00069.

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Ng, Daniel H. J., Jonathan D. Humphries, Adam Byron, Angélique Millon-Frémillon, and Martin J. Humphries. "Microtubule-Dependent Modulation of Adhesion Complex Composition." PLoS ONE 9, no. 12 (2014): e115213. http://dx.doi.org/10.1371/journal.pone.0115213.

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Wan, Andrew C. A., Benjamin C. U. Tai, Karl M. Schumacher, Annegret Schumacher, Sau Yin Chin, and Jackie Y. Ying. "Polyelectrolyte Complex Membranes for Specific Cell Adhesion." Langmuir 24, no. 6 (2008): 2611–17. http://dx.doi.org/10.1021/la7025768.

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WOODFIELD, Richard J., Matthew N. HODGKIN, Nasreen AKHTAR та ін. "The p85 subunit of phosphoinositide 3-kinase is associated with β-catenin in the cadherin-based adhesion complex". Biochemical Journal 360, № 2 (2001): 335–44. http://dx.doi.org/10.1042/bj3600335.

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Cell adhesion is fundamental to establishing and maintaining the discrete tissues in multicellular organisms. Adhesion must be sufficiently strong to preserve tissue architecture, whilst having the capacity to readily dissociate to permit fundamental processes, such as wound repair, to occur. However, very little is known about the signalling mechanisms involved in temporary down-regulation of cell adhesion to facilitate such processes. Cadherins are the principal mediators of cell–cell adhesion in a wide variety of tissues and species and form multi-protein complexes with cytosolic and cytosk

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Galbraith, Catherine G., Kenneth M. Yamada, and Michael P. Sheetz. "The relationship between force and focal complex development." Journal of Cell Biology 159, no. 4 (2002): 695–705. http://dx.doi.org/10.1083/jcb.200204153.

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To adhere and migrate, cells must be capable of applying cytoskeletal force to the extracellular matrix (ECM) through integrin receptors. However, it is unclear if connections between integrins and the ECM are immediately capable of transducing cytoskeletal contraction into migration force, or whether engagement of force transmission requires maturation of the adhesion. Here, we show that initial integrin–ECM adhesions become capable of exerting migration force with the recruitment of vinculin, a marker for focal complexes, which are precursors of focal adhesions. We are able to induce the dev

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Bradley, William D., Samuel E. Hernández, Jeffrey Settleman, and Anthony J. Koleske. "Integrin Signaling through Arg Activates p190RhoGAP by Promoting Its Binding to p120RasGAP and Recruitment to the Membrane." Molecular Biology of the Cell 17, no. 11 (2006): 4827–36. http://dx.doi.org/10.1091/mbc.e06-02-0132.

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The Rho family GTPases RhoA (Rho), Rac1, and Cdc42 are essential effectors of integrin-mediated cell attachment and spreading. Rho activity, which promotes formation of focal adhesions and actin stress fibers, is inhibited upon initial cell attachment to allow sampling of the new adhesive environment. The Abl-related gene (Arg) tyrosine kinase mediates adhesion-dependent inhibition of Rho through phosphorylation and activation of the Rho inhibitor p190RhoGAP-A (p190). p190 phosphorylation promotes its binding to p120RasGAP (p120). Here, we elucidate the mechanism by which p120 binding regulate

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Helwani, Falak M., Eva M. Kovacs, Andrew D. Paterson, et al. "Cortactin is necessary for E-cadherin–mediated contact formation and actin reorganization." Journal of Cell Biology 164, no. 6 (2004): 899–910. http://dx.doi.org/10.1083/jcb.200309034.

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Classical cadherin adhesion molecules are key determinants of cell–cell recognition during development and in post-embryonic life. A decisive step in productive cadherin-based recognition is the conversion of nascent adhesions into stable zones of contact. It is increasingly clear that such contact zone extension entails active cooperation between cadherin adhesion and the force-generating capacity of the actin cytoskeleton. Cortactin has recently emerged as an important regulator of actin dynamics in several forms of cell motility. We now report that cortactin is recruited to cell–cell adhesi

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Lu, X., J. A. Williams, J. J. Deadman та ін. "Preferential antagonism of the interactions of the integrin αIIbβ3 with immobilized glycoprotein ligands by snake-venom RGD (Arg-Gly-Asp) proteins. Evidence supporting a functional role for the amino acid residues flanking the tripeptide RGD in determining the inhibitory properties of snake-venom RGD proteins". Biochemical Journal 304, № 3 (1994): 929–36. http://dx.doi.org/10.1042/bj3040929.

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The inhibitory properties of a panel of snake-venom-derived RGD (Arg-Gly-Asp) proteins, including the disintegrins kistrin, elegantin and albolabrin, and the neurotoxin homologue dendroaspin, were investigated in a platelet-adhesion assay using three immobilized ligands of the glycoprotein IIb-IIIa complex (alpha IIb beta 3), namely fibrinogen, fibronectin and von Willebrand factor (vWF). The snake-venom proteins preferentially inhibited the adhesion of ADP-treated platelets to one or more of the immobilized ligands. Kistrin and dendroaspin exhibited similar inhibitory characteristics, abrogat

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Nelson, W. James. "Regulation of cell–cell adhesion by the cadherin–catenin complex." Biochemical Society Transactions 36, no. 2 (2008): 149–55. http://dx.doi.org/10.1042/bst0360149.

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Ca2+-dependent cell–cell adhesion is regulated by the cadherin family of cell adhesion proteins. Cadherins form trans-interactions on opposing cell surfaces which result in weak cell–cell adhesion. Stronger cell–cell adhesion occurs by clustering of cadherins and through changes in the organization of the actin cytoskeleton. Although cadherins were thought to bind directly to the actin cytoskeleton through cytoplasmic proteins, termed α- and β-catenin, recent studies with purified proteins indicate that the interaction is not direct, and instead an allosteric switch in α-catenin may mediate ac

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Horton, Edward R., Jonathan D. Humphries, Ben Stutchbury, et al. "Modulation of FAK and Src adhesion signaling occurs independently of adhesion complex composition." Journal of Cell Biology 212, no. 3 (2016): 349–64. http://dx.doi.org/10.1083/jcb.201508080.

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Integrin adhesion complexes (IACs) form mechanochemical connections between the extracellular matrix and actin cytoskeleton and mediate phenotypic responses via posttranslational modifications. Here, we investigate the modularity and robustness of the IAC network to pharmacological perturbation of the key IAC signaling components focal adhesion kinase (FAK) and Src. FAK inhibition using AZ13256675 blocked FAKY397 phosphorylation but did not alter IAC composition, as reported by mass spectrometry. IAC composition was also insensitive to Src inhibition using AZD0530 alone or in combination with

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Böttcher, Ralph T., Maik Veelders, Pascaline Rombaut, et al. "Kindlin-2 recruits paxillin and Arp2/3 to promote membrane protrusions during initial cell spreading." Journal of Cell Biology 216, no. 11 (2017): 3785–98. http://dx.doi.org/10.1083/jcb.201701176.

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Cell spreading requires the coupling of actin-driven membrane protrusion and integrin-mediated adhesion to the extracellular matrix. The integrin-activating adaptor protein kindlin-2 plays a central role for cell adhesion and membrane protrusion by directly binding and recruiting paxillin to nascent adhesions. Here, we report that kindlin-2 has a dual role during initial cell spreading: it binds paxillin via the pleckstrin homology and F0 domains to activate Rac1, and it directly associates with the Arp2/3 complex to induce Rac1-mediated membrane protrusions. Consistently, abrogation of kindli

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Maher, Meghan T., Annette S. Flozak, Adam M. Stocker, Anjen Chenn та Cara J. Gottardi. "Activity of the β-catenin phosphodestruction complex at cell–cell contacts is enhanced by cadherin-based adhesion". Journal of Cell Biology 186, № 2 (2009): 219–28. http://dx.doi.org/10.1083/jcb.200811108.

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It is well established that cadherin protein levels impact canonical Wnt signaling through binding and sequestering β-catenin (β-cat) from T-cell factor family transcription factors. Whether changes in intercellular adhesion can affect β-cat signaling and the mechanism through which this occurs has remained unresolved. We show that axin, APC2, GSK-3β and N-terminally phosphorylated forms of β-cat can localize to cell–cell contacts in a complex that is molecularly distinct from the cadherin–catenin adhesive complex. Nonetheless, cadherins can promote the N-terminal phosphorylation of β-cat, and

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Blackstone, B. N., R. Li, W. E. Ackerman, S. N. Ghadiali, H. M. Powell, and D. A. Kniss. "Myoferlin depletion elevates focal adhesion kinase and paxillin phosphorylation and enhances cell-matrix adhesion in breast cancer cells." American Journal of Physiology-Cell Physiology 308, no. 8 (2015): C642—C649. http://dx.doi.org/10.1152/ajpcell.00276.2014.

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Breast cancer is the second leading cause of malignant death among women. A crucial feature of metastatic cancers is their propensity to lose adhesion to the underlying basement membrane as they transition to a motile phenotype and invade surrounding tissue. Attachment to the extracellular matrix is mediated by a complex of adhesion proteins, including integrins, signaling molecules, actin and actin-binding proteins, and scaffolding proteins. Focal adhesion kinase (FAK) is pivotal for the organization of focal contacts and maturation into focal adhesions, and disruption of this process is a ha

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Schaller, Michael D., Jeffrey D. Hildebrand, and J. Thomas Parsons. "Complex Formation with Focal Adhesion Kinase: A Mechanism to Regulate Activity and Subcellular Localization of Src Kinases." Molecular Biology of the Cell 10, no. 10 (1999): 3489–505. http://dx.doi.org/10.1091/mbc.10.10.3489.

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Tyrosine phosphorylation of focal adhesion kinase (FAK) creates a high-affinity binding site for the src homology 2 domain of the Src family of tyrosine kinases. Assembly of a complex between FAK and Src kinases may serve to regulate the subcellular localization and the enzymatic activity of members of the Src family of kinases. We show that simultaneous overexpression of FAK and pp60c-srcor p59fynresults in the enhancement of the tyrosine phosphorylation of a limited number of cellular substrates, including paxillin. Under these conditions, tyrosine phosphorylation of paxillin is largely cell

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Melton, Andrew C., Russell K. Soon, J. Genevieve Park, Luis Martinez, Gregory W. deHart, and Hal F. Yee. "Focal adhesion disassembly is an essential early event in hepatic stellate cell chemotaxis." American Journal of Physiology-Gastrointestinal and Liver Physiology 293, no. 6 (2007): G1272—G1280. http://dx.doi.org/10.1152/ajpgi.00134.2007.

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Chemotaxis (i.e., directed migration) of hepatic stellate cells to areas of inflammation is a requisite event in the liver's response to injury. Previous studies of signaling pathways that regulate stellate cell migration suggest a key role for focal adhesions, but the exact function of these protein complexes in motility remains unclear. Focal adhesions attach a cell to its substrate and therefore must be regulated in a highly coordinated manner during migration. To test the hypothesis that focal adhesion turnover is an essential early event for chemotaxis in stellate cells, we employed a liv

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Kinch, M. S., A. Sanfridson, and C. Doyle. "The protein tyrosine kinase p56lck regulates cell adhesion mediated by CD4 and major histocompatibility complex class II proteins." Journal of Experimental Medicine 180, no. 5 (1994): 1729–39. http://dx.doi.org/10.1084/jem.180.5.1729.

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The CD4 protein is expressed on a subset of human T lymphocytes that recognize antigen in the context of major histocompatibility complex (MHC) class II molecules. Using Chinese hamster ovary (CHO) cells expressing human CD4, we have previously demonstrated that the CD4 protein can mediate cell adhesion by direct interaction with MHC class II molecules. In T lymphocytes, CD4 can also function as a signaling molecule, presumably through its intracellular association with p56lck, a member of the src family of protein tyrosine kinases. In the present report, we show that p56lck can affect cell ad

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Chan, Grace K., John A. McGrath, and Maddy Parsons. "Spatial activation of ezrin by epidermal growth factor receptor and focal adhesion kinase co-ordinates epithelial cell migration." Open Biology 11, no. 8 (2021): 210166. http://dx.doi.org/10.1098/rsob.210166.

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Epidermal growth factor receptor (EGFR) plays a critical role in the promotion of epithelial cell proliferation and migration. Previous studies have suggested a cooperative role between EGFR and integrin signalling pathways that enable efficient adhesion and migration but the mechanisms controlling this remain poorly defined. Here, we show that EGFR forms a complex with focal adhesion kinase in epithelial cells. Surprisingly, this complex enhances local Src activity at focal adhesions to promote phosphorylation of the cytoskeletal adaptor protein ezrin at Y478, leading to actomyosin contractil

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Schimmel, Lilian, and Emma Gordon. "The precise molecular signals that control endothelial cell–cell adhesion within the vessel wall." Biochemical Society Transactions 46, no. 6 (2018): 1673–80. http://dx.doi.org/10.1042/bst20180377.

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Endothelial cell–cell adhesion within the wall of the vasculature controls a range of physiological processes, such as growth, integrity and barrier function. The adhesive properties of endothelial cells are tightly controlled by a complex cascade of signals transmitted from the surrounding environment or from within the cells themselves, with the dynamic nature of cellular adhesion and the regulating signalling networks now beginning to be appreciated. Here, we summarise the current knowledge of the mechanisms controlling endothelial cell–cell adhesion in the developing and mature blood vascu

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Sivasankar, Sanjeevi, Yunxiang Zhang, W. James Nelson, and Steven Chu. "Characterizing the Initial Encounter Complex in Cadherin Adhesion." Structure 17, no. 8 (2009): 1075–81. http://dx.doi.org/10.1016/j.str.2009.06.012.

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Thiery, J. "Cell adhesion in development: a complex signaling network." Current Opinion in Genetics & Development 13, no. 4 (2003): 365–71. http://dx.doi.org/10.1016/s0959-437x(03)00088-1.

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Bistac, S., A. Galliano, and M. Schmitt. "Nanofriction of polymers: the complex role of adhesion." Journal of Physics: Condensed Matter 20, no. 35 (2008): 354015. http://dx.doi.org/10.1088/0953-8984/20/35/354015.

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