Fascin and VASP synergistically increase the Young’s modulus of actin comet tails

Suei, Sandy; Plastino, Julie; Kreplak, Laurent

doi:10.1016/j.jsb.2011.11.009

Cited by 5 publications

(4 citation statements)

References 25 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…A recent study has elucidated that Fscn1 and another actin binding protein, VASP, synergistically increase the growth of the actin comet tail, which plays an important role in clathrin-mediated endocytosis63. However, we found that Fscn1 is dispensable for the formation and pinching off of endocytic vesicles, as indicated by our results showing that TGF-β tpe I receptors are normally internalized from the cell membrane to cytoplasm in Fscn1-depleted cells.…”

Section: Discussionsupporting

confidence: 59%

Fscn1 is required for the trafficking of TGF-β family type I receptors during endoderm formation

Liu

Guan

et al. 2016

Nat Commun

View full text Add to dashboard Cite

Microtubules function in TGF-β signalling by facilitating the cytoplasmic trafficking of internalized receptors and the nucleocytoplasmic shuttling of Smads. However, nothing is known about whether actin filaments are required for these processes. Here we report that zebrafish actin-bundling protein fscn1a is highly expressed in mesendodermal precursors and its expression is directly regulated by the TGF-β superfamily member Nodal. Knockdown or knockout of fscn1a leads to a reduction of Nodal signal transduction and endoderm formation in zebrafish embryos. Fscn1 specifically interacts with TGF-β family type I receptors, and its depletion disrupts the association between receptors and actin filaments and sequesters the internalized receptors into clathrin-coated vesicles. Therefore, Fscn1 acts as a molecular linker between TGF-β family type I receptors and the actin filaments to promote the trafficking of internalized receptors from clathrin-coated vesicles to early endosomes during zebrafish endoderm formation.

show abstract

Section: Discussionsupporting

confidence: 59%

Fscn1 is required for the trafficking of TGF-β family type I receptors during endoderm formation

Liu

Guan

et al. 2016

Nat Commun

View full text Add to dashboard Cite

show abstract

“…However, Ena/VASP could also contribute to mechanical rigidity of bundles, since it is multimeric with filamentous actin binding sites, a common motif in crosslinking proteins. Indeed, Ena/VASP is found to magnify the effect of fascin on network rigidity, perhaps explaining the presence of these two proteins in filopodia (301). However, on their own, Ena/VASP proteins only very modestly increase the rigidity of actin networks, possibly due to the flexibility the Ena/VASP tetramer (101,302).…”

Section: E Parallel Actin Bundlesmentioning

confidence: 99%

Actin Dynamics, Architecture, and Mechanics in Cell Motility

Blanchoin

Boujemaa-Paterski

Sykes

et al. 2014

Physiological Reviews

Self Cite

1,234

1,145

View full text Add to dashboard Cite

Tight coupling between biochemical and mechanical properties of the actin cytoskeleton drives a large range of cellular processes including polarity establishment, morphogenesis, and motility. This is possible because actin filaments are semi-flexible polymers that, in conjunction with the molecular motor myosin, can act as biological active springs or "dashpots" (in laymen's terms, shock absorbers or fluidizers) able to exert or resist against force in a cellular environment. To modulate their mechanical properties, actin filaments can organize into a variety of architectures generating a diversity of cellular organizations including branched or crosslinked networks in the lamellipodium, parallel bundles in filopodia, and antiparallel structures in contractile fibers. In this review we describe the feedback loop between biochemical and mechanical properties of actin organization at the molecular level in vitro, then we integrate this knowledge into our current understanding of cellular actin organization and its physiological roles. I. PREFACE ON ACTIN ORGANIZATION AND CELL MECHANICSAnimal cells (i.e., those without a cell wall) have the ability to change their shape to adapt to their environment, move through narrow spaces, divide, or allow exo-and endocytosis. The machinery of these shape changes relies on the assembly of proteins, in particular actin, a globular protein that polymerizes into filaments of different types of organization: branched and crosslinked networks, parallel bundles, and anti-parallel contractile structures (FIGURE 1A). These different architectures can be envisioned as a series of interconnected active springs and dashpots (green and red symbols in FIGURE 1B, respectively) that act as mechanical elements to drive cell shape changes and motility. The purpose of this review is to correlate recent progress in our understanding of the interplay between biochemical elements and mechanical properties. Instead of describing biochemical and mechanical properties separately, our main goal here is to address piece by piece the integrated feedback loop between biochemistry and mechanics.At the front of the cell, branched and crosslinked networks in a quasi two-dimensional sheet make up the lamellipodium, and are the major engine of cell movement since they push the cell membrane by polymerizing against it (FIGURE 1A, iii). Aligned bundles underlie filopodia that are the fingerlike structures at the front of the cell, important for directional response of the cell (FIGURE 1A, iv). A thin layer of actin, called the cell cortex, coats the plasma membrane at the back and sides of the cell, important for cell shape maintenance and changes (FIGURE 1A, i). The rest of the cell contains a three-dimensional network of crosslinked filaments interspersed with contractile bundles, including stress fibers that connect the cell cytoskeleton to the extracellular matrix via focal adhesion sites (FIGURE 1A, ii). Contraction in the cell is produced by the molecular motor protein myosin. Myosin assembles into anti...

show abstract

“…Suei et al utilized AFM to determine the Young's modulus of phalloidin stabilized comets grown under different conditions. 134 The authors found a linear increase in the Young's modulus for comets grown in the presence of fascin above a critical threshold and a decrease of the initial velocity of the comets. VASP and fascin, in combination, resulted in a stronger increase of the Young's modulus compared to only one of the two proteins, in particular for low concentrations.…”

Section: Indentation Experiments On Cellsmentioning

confidence: 99%

Mapping the mechanical properties of biomaterials on different length scales: depth-sensing indentation and AFM based nanoindentation

et al. 2013

View full text Add to dashboard Cite

The micro-and nanomechanical properties of biomaterials are of central importance as surface elasticity, surface elastic response and adhesion play a central role in a large number of biological processes. They influence, e.g. morphogenesis, self-healing abilities and restoration processes, focal adhesion, motility, mechano-transduction, metastasis and are important for drug delivery applications, and others. These processes address fundamental questions in biology, medicine and diagnostics, pharmaceutical research, archaeology, dental as well as cosmetic applications. With nanoindentation as well as AFM force spectroscopic techniques suitable investigation tools are at hand, which can provide mechanical information on different length scales. The development of both techniques resulted in a broad applicability and the number of examples where both techniques have been used to study (soft) biomaterials rapidly increased during the last years.

show abstract

Fascin and VASP synergistically increase the Young’s modulus of actin comet tails

Cited by 5 publications

References 25 publications

Fscn1 is required for the trafficking of TGF-β family type I receptors during endoderm formation

Fscn1 is required for the trafficking of TGF-β family type I receptors during endoderm formation

Actin Dynamics, Architecture, and Mechanics in Cell Motility

Mapping the mechanical properties of biomaterials on different length scales: depth-sensing indentation and AFM based nanoindentation

Contact Info

Product

Resources

About