... of the cell. We found that α-actinin, a filament crosslinker, is essential for network symmetry to be consistent with extracellular microenvironment symmetry. It is required for the interconnection of transverse arcs with radial fibres to ensure an appropriate balance between forces at cell adhesions...

... the generation of tension at E-cadherin, decreased the strength of cell–cell cohesion in an epithelial cell monolayer and prevented force-dependent recruitment of junctional α-actinin. Application of exogenous force to cell–cell adhesions in a myosin-1c-knockdown cell monolayer fully rescued the localization...

... microtubules are regulated in a time- and region-dependent manner. Here, we show that α-actinin-regulated cortical actin filament integrity is crucial to specify different populations of microtubules during cell division in mammalian cells. Depletion of α-actinin caused aberrant recruitment of centralspindlin...

... Limited 2009 2009 Mechanosensing Stress fibers Zyxin α-actinin Actomyosin contractility Laser nanosurgery Correlative microscopy Viscoelasticity Mechanotransduction, or the mechanism by which cells convert mechanical stimuli into biochemical signals, is an essential element of many...

...Andrew S. Rachlin; Carol A. Otey Palladin is a recently described phosphoprotein with an important role in cytoskeletal organization. The major palladin isoform (90-92 kDa) binds to three actin-associated proteins (ezrin, VASP and α-actinin), suggesting that palladin functions as a cytoskeletal...

... surrounding regions). Interestingly, α5-integrin and α-actinin, but not paxillin, reside in a complex throughout the cell, where they diffuse and flow together, even in regions where they are not organized. During adhesion disassembly some integrins diffuse away slowly, α-actinin undergoes a directed movement...

... in myofibril assembly, we used the yeast two-hybrid system to screen a mouse skeletal muscle cDNA library for proteins capable of binding N-RAP in a eukaryotic cell. From yeast two-hybrid experiments we were able to identify three new N-RAP binding partners: α-actinin, filamin-2, and Krp1 (also called sarcosin...

... to bind to α-actinin in vitro. This interaction was confirmed in yeast and mammalian cells. Studies utilizing the three-hybrid system further indicated that zyxin and LPP compete for the same binding site in α-actinin. This site was mapped to the central rod ofα-actinin, which contains spectrin-like...

...-actinin. The activity of MEK1/2 kinases was needed for consecutive cell migration. This work also defined a new function for α-actinin. Upon IGF-IR activation, green fluorescence protein (GFP)-labeled α-actinin concentrated at the base of actin microspikes. Deletion of the N-terminal actin-binding domain...

... was also required for the microtubule-mediated turnover of adhesive complex sites after nocodazole wash-out, suggesting that calpain may mediate focal complex disassembly downstream of microtubules. Using dual imaging of RFP-zyxin and GFP—α-actinin, we observed a temporal and spatial relationship between α...

...) and viewed using a Bio-Rad 1024 MRC Scanning Confocal Microscope. Cells transiently transfected with pGFP-α-actinin were incubated in growth medium for 32 hours, serum-starved for 16 hours, then replated on FN-coated glass coverslips in 35 mm dishes. Cells on the microscope stage were maintained at 37...

...Nobukazu Araki; Tanenori Hatae; Tesshi Yamada; Setsuo Hirohashi ABSTRACT We have applied fluorescence ratio imaging to the analysis of an actin-binding protein concentration relative to F-actin in macrophages, in order to explore the role of a novel α-actinin isoform, actinin-4, relative...

... we have studied the subcellular distribution and phosphorylation of vinculin and α-actinin, two actin binding proteins of the adherent junctions. We found that during the junctional sealing induced by Ca 2+ , both proteins move towards the cell periphery and, while there is a significant increase...

... with the β1 cytosolic domain is not sufficient to target the integrins to focal adhesions. * Author for correspondence (e-mail: [email protected] ) 03 02 1997 10 04 1997 © 1997 by Company of Biologists 1997 Integrin Focal adhesion Talin α-Actinin Integrins...

... and the cytoskeleton. In this study we have used the yeast two-hybrid system to map the domains on α-catenin that allow it to associate with β-catenin/plakoglobin and with α-actinin. We also identify a region on αactinin that is responsible for its interaction with α-catenin. The yeast two-hybrid data were confirmed...

...Francisco Rivero; Bernd Köppel; Barbara Peracino; Salvatore Bozzaro; Florian Siegert; Cornelis J. Weijer; Michael Schleicher; Richard Albrecht; Angelika A. Noegel ABSTRACT We generated Dictyostelium double mutants lacking the two F-actin crosslinking proteins α-actinin and gelation factor...

... of four adhesion-associated proteins, namely vinculin, talin, α-actinin and actin. Cultured chick lens cells were double labeled for each of the junctional molecules, using fluores-cein- and rhodamine-conjugated antibodies or phalloidin. RET images were acquired with fluorescein excitation and rhodamine...

...Ursula Glück; Avri Ben-Ze’ev ABSTRACT α-Actinin is an abundant actin crosslinking protein, also localized at adherens type junctions. In adhesion plaques, α-actinin can link the actin filaments to integrin via vinculin and talin, or directly by binding to the cytoplasmic domain of β 1 -integrin...

... developmental stages of these cultures were double stained with antibodies to titin in combination with antibodies to α-actin, α-actinin, myosin heavy chain (MHC), nebulin, desmin, and β-tubulin. The first indications of titin expression were found in postmitotic mononuclear myoblasts where it is located...

... had cytoplasmic protrusions or blebs on the basal cell surface. The blebs contained both actin and α-actinin. In epithelia cultured with laminin, the basal cell surface was flat. The actin cortical mat became reorganized within two hours. Actin and-actinin were colocalized in the re-formed basal...