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

Sandy Suei; Julie Plastino; Laurent Kreplak

doi:10.1016/j.jsb.2011.11.009

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

Sandy Suei, Julie Plastino, Laurent Kreplak

Medicine

Medicine

Research output: Contribution to journal › Article › peer-review

6 Citations (Scopus)

Abstract

Cell motility is locally achieved by the interplay between lamellipodia and filopodia at the protrusion sites. The actin cytoskeleton rearranges from a highly branched short filamentous network to well aligned elongated bundles from lamellipodia to filopodia, respectively. This process is governed predominantly by actin binding proteins, VASP and fascin, at the leading edge of migratory cells. Here we use an Arp2/3-complex dependent bead motility assay to study the effect of fascin both on its own and in the presence of VASP. The Young's modulus of phalloidin stabilized comets grown in the presence of fascin increased linearly with concentration above a 0.5. μM threshold. Inversely, the initial velocity of the comets decreased linearly with fascin concentration above the same threshold. Interestingly, VASP and fascin together increased the Young's modulus of the comets compared to those grown in the presence of only one of the two proteins. This effect was most remarkable at low concentration, below 0.5 and 0.15. μM for fascin and VASP, respectively. Our results showed that fascin and VASP work cooperatively to enhance the Young's modulus of the actin network within the comets.

Original language	English
Pages (from-to)	40-45
Number of pages	6
Journal	Journal of Structural Biology
Volume	177
Issue number	1
DOIs	https://doi.org/10.1016/j.jsb.2011.11.009
Publication status	Published - Jan 2012

Bibliographical note

Funding Information:
L.K. dedicates this paper to a great mentor and colleague, Ueli Aebi, who introduced him to the wonders of the actin cytoskeleton. The authors thank Dorothy Schafer for providing capping protein; Ping Li, David O’Neil, and Cindy Leggiadro for their assistance in critical point drying and SEM. S.S. acknowledges support from the Human Frontiers Science Program through a Young investigator Grant awarded to J.P., L.K., and Gijsje Koenderink. L. K. acknowledges support from NSERC and CFI. Appendix A

ASJC Scopus Subject Areas

Structural Biology

PubMed: MeSH publication types

Journal Article
Research Support, Non-U.S. Gov't

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10.1016/j.jsb.2011.11.009

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title = "Fascin and VASP synergistically increase the Young's modulus of actin comet tails",

abstract = "Cell motility is locally achieved by the interplay between lamellipodia and filopodia at the protrusion sites. The actin cytoskeleton rearranges from a highly branched short filamentous network to well aligned elongated bundles from lamellipodia to filopodia, respectively. This process is governed predominantly by actin binding proteins, VASP and fascin, at the leading edge of migratory cells. Here we use an Arp2/3-complex dependent bead motility assay to study the effect of fascin both on its own and in the presence of VASP. The Young's modulus of phalloidin stabilized comets grown in the presence of fascin increased linearly with concentration above a 0.5. μM threshold. Inversely, the initial velocity of the comets decreased linearly with fascin concentration above the same threshold. Interestingly, VASP and fascin together increased the Young's modulus of the comets compared to those grown in the presence of only one of the two proteins. This effect was most remarkable at low concentration, below 0.5 and 0.15. μM for fascin and VASP, respectively. Our results showed that fascin and VASP work cooperatively to enhance the Young's modulus of the actin network within the comets.",

author = "Sandy Suei and Julie Plastino and Laurent Kreplak",

note = "Funding Information: L.K. dedicates this paper to a great mentor and colleague, Ueli Aebi, who introduced him to the wonders of the actin cytoskeleton. The authors thank Dorothy Schafer for providing capping protein; Ping Li, David O{\textquoteright}Neil, and Cindy Leggiadro for their assistance in critical point drying and SEM. S.S. acknowledges support from the Human Frontiers Science Program through a Young investigator Grant awarded to J.P., L.K., and Gijsje Koenderink. L. K. acknowledges support from NSERC and CFI. Appendix A ",

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AU - Kreplak, Laurent

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N2 - Cell motility is locally achieved by the interplay between lamellipodia and filopodia at the protrusion sites. The actin cytoskeleton rearranges from a highly branched short filamentous network to well aligned elongated bundles from lamellipodia to filopodia, respectively. This process is governed predominantly by actin binding proteins, VASP and fascin, at the leading edge of migratory cells. Here we use an Arp2/3-complex dependent bead motility assay to study the effect of fascin both on its own and in the presence of VASP. The Young's modulus of phalloidin stabilized comets grown in the presence of fascin increased linearly with concentration above a 0.5. μM threshold. Inversely, the initial velocity of the comets decreased linearly with fascin concentration above the same threshold. Interestingly, VASP and fascin together increased the Young's modulus of the comets compared to those grown in the presence of only one of the two proteins. This effect was most remarkable at low concentration, below 0.5 and 0.15. μM for fascin and VASP, respectively. Our results showed that fascin and VASP work cooperatively to enhance the Young's modulus of the actin network within the comets.

AB - Cell motility is locally achieved by the interplay between lamellipodia and filopodia at the protrusion sites. The actin cytoskeleton rearranges from a highly branched short filamentous network to well aligned elongated bundles from lamellipodia to filopodia, respectively. This process is governed predominantly by actin binding proteins, VASP and fascin, at the leading edge of migratory cells. Here we use an Arp2/3-complex dependent bead motility assay to study the effect of fascin both on its own and in the presence of VASP. The Young's modulus of phalloidin stabilized comets grown in the presence of fascin increased linearly with concentration above a 0.5. μM threshold. Inversely, the initial velocity of the comets decreased linearly with fascin concentration above the same threshold. Interestingly, VASP and fascin together increased the Young's modulus of the comets compared to those grown in the presence of only one of the two proteins. This effect was most remarkable at low concentration, below 0.5 and 0.15. μM for fascin and VASP, respectively. Our results showed that fascin and VASP work cooperatively to enhance the Young's modulus of the actin network within the comets.

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

Abstract

Bibliographical note

ASJC Scopus Subject Areas

PubMed: MeSH publication types

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