... 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...

... actin bundles. Mechanosensing Stress fibers Zyxin α-actinin Actomyosin contractility Laser nanosurgery Correlative microscopy Viscoelasticity ‡ Author for correspondence (e-mail: julien.colombelli@irbbarcelona.org ) * Present address: Advanced Digital Microscopy, Institute...

...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...

..., 292-294. Y i n , H . L ., J a n m e y , P . A. a n d S c h l e i c h e r , M . (1990). Severin is a gelsolin prototype. FEBS Lett. 264, 78-80. 94 M. Way et al. actin binding proteins α -actinin gelsolin expression homologies © The Company of Biologists Limited 1991 1991 ...