title: Triggering signaling pathways using F-actin self-organization.
abstract: The spatiotemporal organization of proteins within cells is essential for cell fate behavior. Although it is known that the cytoskeleton is vital for numerous cellular functions, it remains unclear how cytoskeletal activity can shape and control signaling pathways in space and time throughout the cell cytoplasm. Here we show that F-actin self-organization can trigger signaling pathways by engineering two novel properties of the microfilament self-organization: (1) the confinement of signaling proteins and (2) their scaffolding along actin polymers. Using in vitro reconstitutions of cellular functions, we found that both the confinement of nanoparticle-based signaling platforms powered by F-actin contractility and the scaffolding of engineered signaling proteins along actin microfilaments can drive a signaling switch. Using Ran-dependent microtubule nucleation, we found that F-actin dynamics promotes the robust assembly of microtubules. Our in vitro assay is a first step towards the development of novel bottom-up strategies to decipher the interplay between cytoskeleton spatial organization and signaling pathway activity.
authors.affiliation: Ecole Normale Supérieure, Department of Chemistry PSL Research University-CNRS-ENS-UPMC 24, rue Lhomond, 75005, Paris, France.
authors.forename: A
authors.initials: A
authors.lastname: Colin
authors.affiliation: Ecole Normale Supérieure, Department of Chemistry PSL Research University-CNRS-ENS-UPMC 24, rue Lhomond, 75005, Paris, France.
authors.forename: L
authors.initials: L
authors.lastname: Bonnemay
authors.affiliation: Ecole Normale Supérieure, Department of Chemistry PSL Research University-CNRS-ENS-UPMC 24, rue Lhomond, 75005, Paris, France.
authors.forename: C
authors.initials: C
authors.lastname: Gayrard
authors.affiliation: Ecole Normale Supérieure, Department of Chemistry PSL Research University-CNRS-ENS-UPMC 24, rue Lhomond, 75005, Paris, France.
authors.forename: J
authors.initials: J
authors.lastname: Gautier
authors.affiliation: Ecole Normale Supérieure, Department of Chemistry PSL Research University-CNRS-ENS-UPMC 24, rue Lhomond, 75005, Paris, France.
authors.forename: Z
authors.initials: Z
authors.lastname: Gueroui
mesh_terms: D008841:Actin Cytoskeleton / Q000378:metabolism* / Q000648:ultrastructure; D000199:Actins / Q000235:genetics / Q000378:metabolism*; D000818:Animals; D005260:Female; D019793:Fluorescein / Q000737:chemistry; D015870:Gene Expression; D017930:Genes, Reporter; D008164:Luminescent Proteins / Q000235:genetics / Q000378:metabolism; D061848:Optical Imaging; D010063:Ovum / Q000378:metabolism* / Q000648:ultrastructure; D012235:Rhodamines / Q000737:chemistry; D015398:Signal Transduction; D014982:Xenopus laevis / Q000378:metabolism; D020931:ran GTP-Binding Protein / Q000235:genetics* / Q000378:metabolism; D000097573:Red Fluorescent Protein
chemical_list: D000199:Actins; D019793:Fluorescein; D008164:Luminescent Proteins; D012235:Rhodamines; D020931:ran GTP-Binding Protein; D000097573:Red Fluorescent Protein