Arp2/3 complex-deficient mouse fibroblasts are viable and have normal leading-edge actin structure and function

Nardo, Alessia Di; Cicchetti, Gregor; Falet, Hervé; Hartwig, John H.; Stossel, Thomas P.; Kwiatkowski, David J.

doi:10.1073/pnas.0508228102

Cited by 55 publications

(61 citation statements)

References 32 publications

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“…The SCAR/ WAVE complex plays an important role in regulating actin filament arrangement by activating the Arp2/3 complex to modify actin filament organization (Blanchoin et al, 2000;Frank et al, 2004;Beltzner and Pollard, 2008). Mutations in key components of the SCAR/ WAVE-Arp2/3 complex result in various defects in yeast and animals (Winter et al, 1999;Di Nardo et al, 2005). In many cases, these mutations cause embryonic arrest and zygotic lethality by impairing various cellular activities (Severson et al, 2002;Sawa et al, 2003;Vartiainen and Machesky, 2004).…”

Section: Discussionmentioning

confidence: 99%

Rice TUTOU1 Encodes a Suppressor of cAMP Receptor-Like Protein That Is Important for Actin Organization and Panicle Development

et al. 2015

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Panicle development, a key event in rice (Oryza sativa) reproduction and a critical determinant of grain yield, forms a branched structure containing multiple spikelets. Genetic and environmental factors can perturb panicle development, causing panicles to degenerate and producing characteristic whitish, small spikelets with severely reduced fertility and yield; however, little is known about the molecular basis of the formation of degenerating panicles in rice. Here, we report the identification and characterization of the rice panicle degenerative mutant tutou1 (tut1), which shows severe defects in panicle development. The tut1 also shows a pleiotropic phenotype, characterized by short roots, reduced plant height, and abnormal development of anthers and pollen grains. Molecular genetic studies revealed that TUT1 encodes a suppressor of cAMP receptor/Wiskott-Aldrich syndrome protein family verprolin-homologous (SCAR/WAVE)-like protein. We found that TUT1 contains conserved functional domains found in eukaryotic SCAR/WAVE proteins, and was able to activate Actin-related protein2/3 to promote actin nucleation and polymerization in vitro. Consistently, tut1 mutants show defects in the arrangement of actin filaments in trichome. These results indicate that TUT1 is a functional SCAR/WAVE protein and plays an important role in panicle development.

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Section: Discussionmentioning

confidence: 99%

Rice TUTOU1 Encodes a Suppressor of cAMP Receptor-Like Protein That Is Important for Actin Organization and Panicle Development

et al. 2015

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“…It is known that Arp2/3 is recruited to nascent integrin adhesions (DeMali et al, 2002;Serrels et al, 2007) and that the actin retrograde flow can transfer myosin II-generated tension to promote adhesion growth and maturation (Galbraith et al, 2002;Choi et al, 2008;Wolfenson et al, 2011). Consequently, we propose that Arp2/3 inhibition reduces the chance for adhesions to interact with the overhead actin network because of its reduced branch density, in turn, leading to reduced tension on adhesions by the retrograde flow, which could reduce their maturation and/or stability.…”

Section: Discussionmentioning

confidence: 99%

“…This multiprotein complex binds to the side of a preexisting actin filament and nucleates an actin branch (Mullins et al, 1997). This branched actin network has been implicated in numerous processes in non-neuronal cells (Goley and Welch, 2006), most commonly associated with lamellipodial formation and protrusion (Suraneni et al, 2012;Wu et al, 2012), though not all reports agree (Di Nardo et al, 2005). Arp2/3 is also required for haptotaxis in fibroblasts, but not chemotaxis (Wu et al, 2012); although, other groups have shown it is required for chemotaxis (Mukai et al, 2005;Suraneni et al, 2012).…”

Section: Introductionmentioning

confidence: 99%

The Role of Arp2/3 in Growth Cone Actin Dynamics and Guidance Is Substrate Dependent

Miguel-Ruiz

Letourneau

2014

J. Neurosci.

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During development extrinsic guidance cues modulate the peripheral actin network in growth cones to direct axons to their targets. We wanted to understand the role of the actin nucleator Arp2/3 in growth cone actin dynamics and guidance. Since growth cones migrate in association with diverse adhesive substrates during development, we probed the hypothesis that the functional significance of Arp2/3 is substrate dependent. We report that Arp2/3 inhibition led to a reduction in the number of filopodia and growth cone F-actin content on laminin and L1. However, we found substrate-dependent differences in growth cone motility, actin retrograde flow, and guidance after Arp2/3 inhibition, suggesting that its role, and perhaps that of other actin binding proteins, in growth cone motility is substrate dependent.

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“…Reconstituted motility assays also enabled controlled measurements of the force produced by actin polymerization (30). WASP family proteins use Arp2/3 complex to branch filaments at the leading edge, whereas formins may contribute to lamellipodium or filopodium or nerve growth cone extension or even supplement the absence of Arp2/3 (31,32).…”

Section: Insight Into the Mechanism Of Actin-based Motility From Recomentioning

confidence: 99%

Control of Actin Assembly Dynamics in Cell Motility

Carlier

Pantaloni

2007

Journal of Biological Chemistry

162

134

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Motile processes at the origin of cell migration, cell division, synaptic plasticity, and endocytosis, but also morphogenetic processes that define anterior-posterior and ventral-dorsal polarity of the embryo, or left-right asymmetry, are driven by spatially and temporally controlled assembly of actin filaments (1-4). Cell biological studies and reconstituted motility assays indicate that polarized filament barbed end growth, at specific sites on the membrane, generates the forces responsible for lamellipodia and filopodia extension, as well as tensile forces that strengthen focal adhesions. Fluorescence speckle microscopy of actin and regulatory proteins in motile cells show that morphologically and dynamically distinct networks of actin filaments initiated at the plasma membrane coexist in the cell and define cellular compartments (5, 6). How are these different turnover rates coordinated to achieve directional movement in response to extracellular cues? How can regulatory proteins recognize distinct actin networks? What are the relationships between the force produced by filament barbed end growth that deforms the membrane and the molecular mechanism of the protein machineries that link barbed ends to the membrane? New insights into these issues have emerged from recent cellular, physical, and biochemical approaches.

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Arp2/3 complex-deficient mouse fibroblasts are viable and have normal leading-edge actin structure and function

Cited by 55 publications

References 32 publications

Rice TUTOU1 Encodes a Suppressor of cAMP Receptor-Like Protein That Is Important for Actin Organization and Panicle Development

Rice TUTOU1 Encodes a Suppressor of cAMP Receptor-Like Protein That Is Important for Actin Organization and Panicle Development

The Role of Arp2/3 in Growth Cone Actin Dynamics and Guidance Is Substrate Dependent

Control of Actin Assembly Dynamics in Cell Motility

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