Formins filter modified actin subunits during processive elongation.
TLDR
Formin Cdc12p rejects actin subunits with a tag of ~2 kDa, illustrating the stringent structural requirements for this formin to promote the elongation of actin filament barbed ends as it moves processively along the end of a growing filament.About:
This article is published in Journal of Structural Biology.The article was published on 2012-01-01 and is currently open access. It has received 82 citations till now. The article focuses on the topics: Arp2/3 complex & MDia1.read more
Citations
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Journal ArticleDOI
Actin Dynamics, Architecture, and Mechanics in Cell Motility
TL;DR: The feedback loop between biochemical and mechanical properties of actin organization at the molecular level in vitro is described and this knowledge is integrated into the current understanding of cellular actin organizations and its physiological roles.
Journal ArticleDOI
DNA damage induces nuclear actin filament assembly by Formin-2 and Spire-1/2 that promotes efficient DNA repair
TL;DR: It is found that DNA damage also generates nuclear actin filaments—detectable by phalloidin and live-cell actin probes—with three characteristic morphologies: (i) long, nucleoplasmic filaments; (ii) short, nucleolus-associated filament; and (iii) dense, nucleopa clusters.
Journal ArticleDOI
The Cytoskeleton-A Complex Interacting Meshwork.
Tim Hohmann,Faramarz Dehghani +1 more
TL;DR: The findings about cytoskeletal filament types, including substructures formed by them, such as lamellipodia, stress fibers, and interactions between intermediate filaments, microtubules and actin are summarized.
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Formin-generated actomyosin arcs propel T cell receptor microcluster movement at the immune synapse.
Sricharan Murugesan,Jinsung Hong,Jason Yi,Dong Li,Dong Li,Jordan R. Beach,Lin Shao,John Meinhardt,Grey P. Madison,Xufeng Wu,Eric Betzig,John A. Hammer +11 more
TL;DR: The authors reveal the origin, organization, and functions of a major cytoskeletal network during synapse maturation and report that actomyosin arcs at the T cell synapse are formin-generated structures that directly propel T cell receptor cluster movement.
Journal ArticleDOI
A transient pool of nuclear F-actin at mitotic exit controls chromatin organization
Christian Baarlink,Matthias Plessner,Alice Sherrard,Kohtaro Morita,Shinji Misu,David Virant,Eva-Maria Kleinschnitz,Robert L. Harniman,Dominic Alibhai,Stefan Baumeister,Kei Miyamoto,Ulrike Endesfelder,Abderrahmane Kaidi,Robert Grosse +13 more
TL;DR: The transient formation of nuclear actin filaments (F-actin) during mitotic exit is described, identifying a cell-cycle-specific and spatiotemporally controlled form of nuclear F- actin that reorganizes the mammalian nucleus after mitosis.
References
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The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling
TL;DR: The SWISS-MODEL workspace is a web-based integrated service dedicated to protein structure homology modelling that assists and guides the user in building protein homology models at different levels of complexity.
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Lifeact: a versatile marker to visualize F-actin
Julia Riedl,Alvaro H. Crevenna,Kai Kessenbrock,Jerry Haochen Yu,Dorothee Neukirchen,Michal Bista,Frank Bradke,Dieter E. Jenne,Tad A. Holak,Zena Werb,Michael Sixt,Roland Wedlich-Söldner +11 more
TL;DR: Lifeact, a 17-amino-acid peptide, is described, which stained filamentous actin (F-actin) structures in eukaryotic cells and tissues and in its chemically modified peptide form allowed visualization of actin dynamics in nontransfectable cells.
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The SWISS-MODEL Repository and associated resources
TL;DR: The aim of the SWISS-MODEL Repository is to provide access to an up-to-date collection of annotated 3D protein models generated by automated homology modelling for all sequences in Swiss-Prot and for relevant models organisms.
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Specific Covalent Labeling of Recombinant Protein Molecules Inside Live Cells
TL;DR: This system provides a recipe for slightly modifying a target protein so that it can be singled out from the many other proteins inside live cells and fluorescently stained by small nonfluorescent dye molecules added from outside the cells.
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New biarsenical ligands and tetracysteine motifs for protein labeling in vitro and in vivo: synthesis and biological applications.
Stephen R. Adams,Robert E. Campbell,Larry A. Gross,Brent R. Martin,Grant K. Walkup,Yong Yao,Juan Llopis,Roger Y. Tsien +7 more
TL;DR: Affinities in vitro and detection limits in living cells are optimized with Xaa-Xaa = Pro-Gly, suggesting that the preferred peptide conformation is a hairpin rather than the previously proposed alpha-helix.
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