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https://www.readbyqxmd.com/read/27922008/defining-functional-interactions-during-biogenesis-of-epithelial-junctions
#1
J C Erasmus, S Bruche, L Pizarro, N Maimari, T Pogglioli, C Tomlinson, J Lees, I Zalivina, A Wheeler, A Alberts, A Russo, V M M Braga
In spite of extensive recent progress, a comprehensive understanding of how actin cytoskeleton remodelling supports stable junctions remains to be established. Here we design a platform that integrates actin functions with optimized phenotypic clustering and identify new cytoskeletal proteins, their functional hierarchy and pathways that modulate E-cadherin adhesion. Depletion of EEF1A, an actin bundling protein, increases E-cadherin levels at junctions without a corresponding reinforcement of cell-cell contacts...
December 6, 2016: Nature Communications
https://www.readbyqxmd.com/read/27919746/fhod1-formin-is-upregulated-in-melanomas-and-modifies-proliferation-and-tumor-growth
#2
Minna Peippo, Maria Gardberg, Tarja Lamminen, Katja Kaipio, Olli Carpén, Vanina D Heuser
The functional properties of actin-regulating formin proteins are diverse and in many cases cell-type specific. FHOD1, a formin expressed predominantly in cells of mesenchymal lineage, bundles actin filaments and participates in maintenance of cell shape, migration and cellular protrusions. FHOD1 participates in cancer-associated epithelial to mesenchymal transition (EMT) in oral squamous cell carcinoma and breast cancer. The role of FHOD1 in melanomas has not been characterized. Here, we show that FHOD1 expression is typically strong in cutaneous melanomas and cultured melanoma cells while the expression is low or absent in benign nevi...
December 2, 2016: Experimental Cell Research
https://www.readbyqxmd.com/read/27919320/calcium-mediated-actin-reset-caar-mediates-acute-cell-adaptations
#3
Pauline Wales, Christian E Schuberth, Roland Aufschnaiter, Johannes Fels, Ireth García-Aguilar, Annette Janning, Christopher P Dlugos, Marco Schäfer-Herte, Christoph Klingner, Mike Wälte, Julian Kuhlmann, Ekaterina Menis, Laura Hockaday Kang, Kerstin C Maier, Wenya Hou, Antonella Russo, Henry N Higgs, Hermann Pavenstädt, Thomas Vogl, Johannes Roth, Britta Qualmann, Michael M Kessels, Dietmar E Martin, Bela Mulder, Roland Wedlich-Söldner
Actin has well established functions in cellular morphogenesis. However, it is not well understood how the various actin assemblies in a cell are kept in a dynamic equilibrium, in particular when cells have to respond to acute signals. Here, we characterize a rapid and transient actin reset in response to increased intracellular calcium levels. Within seconds of calcium influx, the formin INF2 stimulates filament polymerization at the endoplasmic reticulum (ER), while cortical actin is disassembled. The reaction is then reversed within a few minutes...
December 6, 2016: ELife
https://www.readbyqxmd.com/read/27913680/new-nuclear-and-perinuclear-functions-of-formins
#4
REVIEW
Tadamoto Isogai, Metello Innocenti
Formin family proteins (formins) represent an evolutionary conserved protein family encoded in the genome of a wide range of eukaryotes. Formins are hallmarked by a formin homology 1 (FH1) domain juxtaposed to an FH2 domain whereby they control actin and microtubule dynamics. Not surprisingly, formins are best known as key regulators of the cytoskeleton in a variety of morphogenetic processes. However, mounting evidence implicates several formins in the assembly and organization of actin within and around the nucleus...
December 15, 2016: Biochemical Society Transactions
https://www.readbyqxmd.com/read/27912053/formin-a-nuclear-protection
#5
Jörg Renkawitz, Michael Sixt
In this issue of Cell, Skau et al. show that the formin FMN2 organizes a perinuclear actin cytoskeleton that protects the nucleus and its genomic content of migrating cells squeezing through small spaces.
December 1, 2016: Cell
https://www.readbyqxmd.com/read/27911711/diaphanous-related-formin-1-as-a-target-for-tumor-therapy
#6
REVIEW
Yuan-Na Lin, Sabine Windhorst
Formins nucleate actin and stabilize microtubules (MTs). Expression of the formin Diaphanous homolog 1 (DIAPH1) is increased in malignant colon carcinoma cells, while expression of DIAPH3 is up-regulated in breast and prostate carcinoma cells. Both DIAPH1 isoforms are required to stabilize interphase MTs of cancer cells, and it has been shown that loss of this function decreases the metastatic potential of these cells. Moreover, depletion of DIAPH3 increases the sensitivity of breast and prostate carcinoma cells to taxanes...
October 15, 2016: Biochemical Society Transactions
https://www.readbyqxmd.com/read/27866892/tropomyosin-and-profilin-cooperate-to-promote-formin-mediated-actin-nucleation-and-drive-yeast-actin-cable-assembly
#7
Salvatore L Alioto, Mikael V Garabedian, Danielle R Bellavance, Bruce L Goode
Tropomyosins comprise a large family of actin-binding proteins with critical roles in diverse actin-based processes [1], but our understanding of how they mechanistically contribute to actin filament dynamics has been limited. We addressed this question in S. cerevisiae, where tropomyosins (Tpm1 and Tpm2), profilin (Pfy1), and formins (Bni1 and Bnr1) are required for the assembly of an array of actin cables that facilitate polarized vesicle delivery and daughter cell growth. Formins drive cable formation by promoting actin nucleation and by accelerating actin filament elongation together with profilin [2]...
November 15, 2016: Current Biology: CB
https://www.readbyqxmd.com/read/27858184/pathogenic-mechanisms-of-actin-cross-linking-toxins-peeling-away-the-layers
#8
Elena Kudryashova, David B Heisler, Dmitri S Kudryashov
Actin cross-linking toxins are produced by Gram-negative bacteria from Vibrio and Aeromonas genera. The toxins were named actin cross-linking domains (ACD), since the first and most of the subsequently discovered ACDs were found as effector domains in larger MARTX and VgrG toxins. Among recognized human pathogens, ACD is produced by Vibrio cholerae, Vibrio vulnificus, and Aeromonas hydrophila. Upon delivery to the cytoplasm of a host cell, ACD covalently cross-links actin monomers into non-polymerizable actin oligomers of various lengths...
November 18, 2016: Current Topics in Microbiology and Immunology
https://www.readbyqxmd.com/read/27851961/wip-drives-tumor-progression-through-yap-taz-dependent-autonomous-cell-growth
#9
Ricardo Gargini, Maribel Escoll, Esther García, Ramón García-Escudero, Francisco Wandosell, Inés María Antón
In cancer, the deregulation of growth signaling pathways drives changes in the cell's architecture and its environment that allow autonomous growth of tumors. These cells then acquire a tumor-initiating "stemness" phenotype responsible for disease advancement to more aggressive stages. Here, we show that high levels of the actin cytoskeleton-associated protein WIP (WASP-interacting protein) correlates with tumor growth, both of which are linked to the tumor-initiating cell phenotype. We find that WIP controls tumor growth by boosting signals that stabilize the YAP/TAZ complex via a mechanism mediated by the endocytic/endosomal system...
November 15, 2016: Cell Reports
https://www.readbyqxmd.com/read/27848932/lack-of-diaph3-relaxes-the-spindle-checkpoint-causing-the-loss-of-neural-progenitors
#10
Devid Damiani, André M Goffinet, Arthur Alberts, Fadel Tissir
The diaphanous homologue Diaph3 (aka mDia2) is a major regulator of actin cytoskeleton. Loss of Diaph3 has been constantly associated with cytokinesis failure ascribed to impaired accumulation of actin in the cleavage furrow. Here we report that Diaph3 is required before cell fission, to ensure the accurate segregation of chromosomes. Inactivation of the Diaph3 gene causes a massive loss of cortical progenitor cells, with subsequent depletion of intermediate progenitors and neurons, and results in microcephaly...
November 16, 2016: Nature Communications
https://www.readbyqxmd.com/read/27821733/a-diaphanous-related-formin-links-ras-signaling-directly-to-actin-assembly-in-macropinocytosis-and-phagocytosis
#11
Alexander Junemann, Vedrana Filić, Moritz Winterhoff, Benjamin Nordholz, Christof Litschko, Helena Schwellenbach, Till Stephan, Igor Weber, Jan Faix
Phagocytosis and macropinocytosis are Ras-regulated and actin-driven processes that depend on the dynamic rearrangements of the plasma membrane that protrudes and internalizes extracellular material by cup-shaped structures. However, the regulatory mechanisms underlying actin assembly in large-scale endocytosis remain elusive. Here, we show that the Diaphanous-related formin G (ForG) from the professional phagocyte Dictyostelium discoideum localizes to endocytic cups. Biochemical analyses revealed that ForG is a rather weak nucleator but efficiently elongates actin filaments in the presence of profilin...
November 22, 2016: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/27807130/daam1-stabilizes-epithelial-junctions-by-restraining-wave-complex-dependent-lateral-membrane-motility
#12
Tamako Nishimura, Shoko Ito, Hiroko Saito, Sylvain Hiver, Kenta Shigetomi, Junichi Ikenouchi, Masatoshi Takeichi
Epithelial junctions comprise two subdomains, the apical junctional complex (AJC) and the adjacent lateral membrane contacts (LCs), that span the majority of the junction. The AJC is lined with circumferential actin cables, whereas the LCs are associated with less-organized actin filaments whose roles are elusive. We found that DAAM1, a formin family actin regulator, accumulated at the LCs, and its depletion caused dispersion of actin filaments at these sites while hardly affecting circumferential actin cables...
November 2, 2016: Journal of Cell Biology
https://www.readbyqxmd.com/read/27799367/formin-generated-actomyosin-arcs-propel-t-cell-receptor-microcluster-movement-at-the-immune-synapse
#13
Sricharan Murugesan, Jinsung Hong, Jason Yi, Dong Li, Jordan R Beach, Lin Shao, John Meinhardt, Grey Madison, Xufeng Wu, Eric Betzig, John A Hammer
Actin assembly and inward flow in the plane of the immunological synapse (IS) drives the centralization of T cell receptor microclusters (TCR MCs) and the integrin leukocyte functional antigen 1 (LFA-1). Using structured-illumination microscopy (SIM), we show that actin arcs populating the medial, lamella-like region of the IS arise from linear actin filaments generated by one or more formins present at the IS distal edge. After traversing the outer, Arp2/3-generated, lamellipodia-like region of the IS, these linear filaments are organized by myosin II into antiparallel concentric arcs...
November 7, 2016: Journal of Cell Biology
https://www.readbyqxmd.com/read/27792274/computational-simulation-of-formin-mediated-actin-polymerization-predicts-homologue-dependent-mechanosensitivity
#14
Derek Bryant, Lara Clemens, Jun Allard
Many actin structures are nucleated and assembled by the barbed-end tracking polymerase formin family, including filopodia, focal adhesions, the cytokinetic ring and cell cortex. These structures respond to forces in distinct ways. Formins typically have profilin-actin binding sites embedded in highly flexible disordered FH1 domains, hypothesized to diffusively explore space to rapidly capture actin monomers for delivery to the barbed end. Recent experiments demonstrate that formin mediated polymerization accelerates when under tension...
October 28, 2016: Cytoskeleton
https://www.readbyqxmd.com/read/27789627/filamin-a-and-formin-2-dependent-endocytosis-regulates-proliferation-via-the-canonical-wnt-pathway
#15
Gewei Lian, Markus Dettenhofer, Jie Lu, Michael Downing, Anjen Chenn, Timothy Wong, Volney Sheen
Actin-associated proteins regulate multiple cellular processes, including proliferation and differentiation, but the molecular mechanisms underlying these processes are unclear. Here, we report that the actin-binding protein filamin A (FlnA) physically interacts with the actin-nucleating protein formin 2 (Fmn2). Loss of FlnA and Fmn2 impairs proliferation, thereby generating multiple embryonic phenotypes, including microcephaly. FlnA interacts with the Wnt co-receptor Lrp6. Loss of FlnA and Fmn2 impairs Lrp6 endocytosis, downstream Gsk3β activity, and β-catenin accumulation in the nucleus...
December 1, 2016: Development
https://www.readbyqxmd.com/read/27770600/inf2-and-fhod-related-formins-promote-ovulation-in-the-somatic-gonad-of-c-elegans
#16
Anna Hegsted, Forrest A Wright, SarahBeth Votra, David Pruyne
Formins are regulators of actin filament dynamics. We demonstrate here that two formins, FHOD-1 and EXC-6, are important in the nematode Caenorhabditis elegans for ovulation, during which actomyosin contractions push a maturing oocyte from the gonad arm into a distensible bag-like organ, the spermatheca. EXC-6, a homolog of the disease-associated mammalian formin INF2, is highly expressed in the spermatheca, where it localizes to cell-cell junctions and to circumferential actin filament bundles. Loss of EXC-6 does not noticeably affect the organization the actin filament bundles, and causes only a very modest increase in the population of junction-associated actin filaments...
October 22, 2016: Cytoskeleton
https://www.readbyqxmd.com/read/27769112/quantitative-proteomics-illuminates-a-functional-interaction-between-mdia2-and-the-proteasome
#17
Tadamoto Isogai, Rob van der Kammen, Onno B Bleijerveld, Soenita S Goerdayal, Elisabetta Argenzio, A F Maarten Altelaar, Metello Innocenti
Formin mDia2 is a cytoskeleton-regulatory protein that switches reversibly between a closed, auto-inhibited and an open, active conformation. Although the open conformation of mDia2 induces actin assembly thereby controlling many cellular processes, mDia2 possesses also actin-independent and conformation-insensitive scaffolding roles related to microtubules and p53, respectively. Thus, we hypothesise that mDia2 may have other unappreciated functions and regulatory modes. Here we identify and validate proteasome and Ubiquitin as mDia2-interacting partners using SILAC-based quantitative proteomics and biochemistry, respectively...
October 21, 2016: Journal of Proteome Research
https://www.readbyqxmd.com/read/27760153/formin-daam1-organizes-actin-filaments-in-the-cytoplasmic-nodal-actin-network
#18
Weiwei Luo, Zi Zhao Lieu, Ed Manser, Alexander D Bershadsky, Michael P Sheetz
A nodal cytoplasmic actin network underlies actin cytoplasm cohesion in the absence of stress fibers. We previously described such a network that forms upon Latrunculin A (LatA) treatment, in which formin DAAM1 was localized at these nodes. Knock down of DAAM1 reduced the mobility of actin nodes but the nodes remained. Here we have investigated DAAM1 containing nodes after LatA washout. DAAM1 was found to be distributed between the cytoplasm and the plasma membrane. The membrane binding likely occurs through an interaction with lipid rafts, but is not required for F-actin assembly...
2016: PloS One
https://www.readbyqxmd.com/read/27744511/actin-dependent-regulation-of-borrelia-burgdorferi-phagocytosis-by-macrophages
#19
Xenia Naj, Stefan Linder
The spirochete Borrelia burgdorferi is the causative agent of Lyme disease, a multisystemic disorder affecting primarily skin, nervous system, and joints. If an infection with Borrelia proceeds unchecked, the disease can also enter a chronic stage, leading to the development of neuroborreliosis or cardiac arrhythmia. Successful elimination of B. burgdorferi by the host immune system is thus decisive for the positive outcome of a respective infection. Accordingly, host immune cells such as macrophages and dendritic cells have to be able to efficiently internalize and degrade infecting spirochetes...
October 16, 2016: Current Topics in Microbiology and Immunology
https://www.readbyqxmd.com/read/27731794/the-drosophila-formin-fhos-is-a-primary-mediator-of-sarcomeric-thin-filament-array-assembly
#20
Arkadi Shwartz, Nagaraju Dhanyasi, Eyal D Schejter, Ben-Zion Shilo
Actin-based thin filament arrays constitute a fundamental core component of muscle sarcomeres. We have used formation of the Drosophila indirect flight musculature for studying the assembly and maturation of thin-filament arrays in a skeletal muscle model system. Employing GFP-tagged actin monomer incorporation, we identify several distinct phases in the dynamic construction of thin-filament arrays. This sequence includes assembly of nascent arrays after an initial period of intensive microfilament synthesis, followed by array elongation, primarily from filament pointed-ends, radial growth of the arrays via recruitment of peripheral filaments and continuous barbed-end turnover...
October 12, 2016: ELife
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