Actin-cytoskeleton dynamics in non-monotonic cell spreading

Heinrich, Doris; Youssef, Simon; Schroth‐Diez, Britta; Engel, Ulrike; Aydin, Daniel; Blümmel, Jacques; Spatz, Joachim P.; Gerisch, Günther

doi:10.4161/cam.2.2.6190

Cited by 26 publications

(22 citation statements)

References 51 publications

(71 reference statements)

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“…2(A)], a loose actin network occupied the substrate-attached cell surface as previously described (Diez et al, 2005). Inserted into this network were densely packed actin filaments at leading edges and in patches distributed over the cell surface, the majority of these patches known to be involved in clathrin-dependent endocytosis (Heinrich et al, 2008). In cells recovering from treatment with latrunculin A, waves were the most prominent actin structures.…”

Section: Actin Waves Separate Two States Of Actin Texturementioning

confidence: 87%

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Propagating waves separate two states of actin organization in living cells

et al. 2009

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Propagating actin waves are dynamic supramolecular structures formed by the self-assembly of proteins within living cells. They are built from actin filaments together with single-headed myosin, the Arp23 complex, and coronin in a defined three-dimensional order. The function of these waves in structuring the cell cortex is studied on the substrate-attached surface of Dictyostelium cells by the use of total internal reflection fluorescence (TIRF) microscopy. Actin waves separate two areas of the cell cortex from each other, which are distinguished by the arrangement of actin filaments. The Arp23 complex dominates in the area enclosed by a wave, where it has the capacity of building dendritic structures, while the proteins prevailing in the external area, cortexillin I and myosin-II, bundle actin filaments and arrange them in antiparallel direction. Wave propagation is accompanied by transitions in the state of actin with a preferential period of 5 min. Wave generation is preceded by local fluctuations in actin assembly, some of the nuclei of polymerized actin emanating from clathrin-coated structures, others emerging independently. The dynamics of phase transitions has been analyzed to provide a basis for modeling the nonlinear interactions that produce spatio-temporal patterns in the actin system of living cells.

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Section: Actin Waves Separate Two States Of Actin Texturementioning

confidence: 87%

“…In migrating cells of Dictyostelium, actin waves are formed as one of many other actinbased structures at the substrate-attached surface (Bretschneider et al, 2004), in particular, on strongly adhesive substrates (Heinrich et al, 2008). The generation of these waves is selectively enhanced in a stage of recovery from the complete depolymerization of actin.…”

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confidence: 99%

Propagating waves separate two states of actin organization in living cells

et al. 2009

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“…A Coronin protein displays an inhibitory effect on the steady state of F-actin, and is partially localized to sites of actin polymerization, specifically the decaying ends of actin tails [309]. The F-actin filament severing protein cofilin helps F-actin form appropriate bundles by increasing turnover rates and localizes at the leading edge of a protrusion within 30-60 sec after the 20 sec peak [310,311].…”

Section: Chemotactic Network Of Dictyostelium and Leukocytesmentioning

confidence: 99%

Moving towards a paradigm: common mechanisms of chemotactic signaling in Dictyostelium and mammalian leukocytes

Artemenko

Lampert

Devreotes

2014

Cell. Mol. Life Sci.

178

221

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Chemotaxis, or directed migration of cells along a chemical gradient, is a highly coordinated process that involves gradient sensing, motility, and polarity. Most of our understanding of chemotaxis comes from studies of cells undergoing amoeboid-type migration, in particular the social amoeba Dictyostelium discoideum and leukocytes. In these amoeboid cells the molecular events leading to directed migration can be conceptually divided into four interacting networks: receptor/G protein, signal transduction, cytoskeleton, and polarity. The signal transduction network occupies a central position in this scheme as it receives direct input from the receptor/G protein network, as well as feedback from the cytoskeletal and polarity networks. Multiple overlapping modules within the signal transduction network transmit the signals to the actin cytoskeleton network leading to biased pseudopod protrusion in the direction of the gradient. The overall architecture of the networks, as well as the individual signaling modules are remarkably conserved between Dictyostelium and mammalian leukocytes, and the similarities and differences between the two systems are the subject of this review.

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“…Once activated by phosphorylation, Hip1r could directly regulate and orient actin filament formation, or act as a scaffold to recruit other proteins that regulate actin. Whether direct or not, this pathway probably involves the protein Arp2/3, a key regulator of polymerization of actin filaments that interacts with many proteins involved in clathrin-mediated endocytosis via N-WASP and localizes to internalizing clathrin pits in Dictyostelium and a wide range of other eukaryotes (Schafer, 2002;Merrifield et al, 2004;Heinrich et al, 2008;Yamada et al, 2009). Understanding how this regulatory pathway functions will be key to understanding the complexity of how clathrin-coated pits are integrated with the dynamic actin cytoskeleton.…”

Section: Hip1r Regulates the Coupling Of Actin To Clathrin-coated Pitsmentioning

confidence: 99%

Regulation of Hip1r by epsin controls the temporal and spatial coupling of actin filaments to clathrin-coated pits

Brady

Damer

Heuser

et al. 2010

Journal of Cell Science

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SummaryRecently, it has become clear that the actin cytoskeleton is involved in clathrin-mediated endocytosis. During clathrin-mediated endocytosis, clathrin triskelions and adaptor proteins assemble into lattices, forming clathrin-coated pits. These coated pits invaginate and detach from the membrane, a process that requires dynamic actin polymerization. We found an unexpected role for the clathrin adaptor epsin in regulating actin dynamics during this late stage of coated vesicle formation. In Dictyostelium cells, epsin is required for both the membrane recruitment and phosphorylation of the actin-and clathrin-binding protein Hip1r. Epsin-null and Hip1r-null cells exhibit deficiencies in the timing and organization of actin filaments at clathrin-coated pits. Consequently, clathrin structures persist on the membranes of epsin and Hip1r mutants and the internalization of clathrin structures is delayed. We conclude that epsin works with Hip1r to regulate actin dynamics by controlling the spatial and temporal coupling of actin filaments to clathrin-coated pits. Specific residues in the ENTH domain of epsin that are required for the membrane recruitment and phosphorylation of Hip1r are also required for normal actin and clathrin dynamics at the plasma membrane. We propose that epsin promotes the membrane recruitment and phosphorylation of Hip1r, which in turn regulates actin polymerization at clathrin-coated pits.

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Actin-cytoskeleton dynamics in non-monotonic cell spreading

Cited by 26 publications

References 51 publications

Propagating waves separate two states of actin organization in living cells

Propagating waves separate two states of actin organization in living cells

Moving towards a paradigm: common mechanisms of chemotactic signaling in Dictyostelium and mammalian leukocytes

Regulation of Hip1r by epsin controls the temporal and spatial coupling of actin filaments to clathrin-coated pits

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