title: Super-resolution microscopy reveals LINC complex recruitment at nuclear indentation sites.
abstract: Increasing evidences show that the actin cytoskeleton is a key parameter of the nuclear remodeling process in response to the modifications of cellular morphology. However, detailed information on the interaction between the actin cytoskeleton and the nuclear lamina was still lacking. We addressed this question by constraining endothelial cells on rectangular fibronectin-coated micropatterns and then using Structured Illumination Microscopy (SIM) to observe the interactions between actin stress fibers, nuclear lamina and LINC complexes at a super-resolution scale. Our results show that tension in apical actin stress fibers leads to deep nuclear indentations that significantly deform the nuclear lamina. Interestingly, indented nuclear zones are characterized by a local enrichment of LINC complexes, which anchor apical actin fibers to the nuclear lamina. Moreover, our findings indicate that nuclear indentations induce the formation of segregated domains of condensed chromatin. However, nuclear indentations and condensed chromatin domains are not irreversible processes and both can relax in absence of tension in apical actin stress fibers.
authors.affiliation: Mechanobiology &Soft Matter Group, Interfaces and Complex Fluids Laboratory, Research Institute for Biosciences, CIRMAP, University of Mons, 20 Place du Parc B-7000 Mons, Belgium.
authors.forename: Marie
authors.initials: M
authors.lastname: Versaevel
authors.affiliation: Nikon Belux Instruments, 50 B Avenue du Bourget, B-1130 Brussels, Belgium.
authors.forename: Jean-Baptiste
authors.initials: JB
authors.lastname: Braquenier
authors.affiliation: Mechanobiology &Soft Matter Group, Interfaces and Complex Fluids Laboratory, Research Institute for Biosciences, CIRMAP, University of Mons, 20 Place du Parc B-7000 Mons, Belgium.
authors.forename: Maryam
authors.initials: M
authors.lastname: Riaz
authors.affiliation: Mechanobiology &Soft Matter Group, Interfaces and Complex Fluids Laboratory, Research Institute for Biosciences, CIRMAP, University of Mons, 20 Place du Parc B-7000 Mons, Belgium.
authors.forename: Thomas
authors.initials: T
authors.lastname: Grevesse
authors.affiliation: Mechanobiology &Soft Matter Group, Interfaces and Complex Fluids Laboratory, Research Institute for Biosciences, CIRMAP, University of Mons, 20 Place du Parc B-7000 Mons, Belgium.
authors.forename: Joséphine
authors.initials: J
authors.lastname: Lantoine
authors.affiliation: Mechanobiology &Soft Matter Group, Interfaces and Complex Fluids Laboratory, Research Institute for Biosciences, CIRMAP, University of Mons, 20 Place du Parc B-7000 Mons, Belgium.
authors.forename: Sylvain
authors.initials: S
authors.lastname: Gabriele
mesh_terms: D002467:Cell Nucleus; D002843:Chromatin / Q000378:metabolism; D003599:Cytoskeleton / Q000378:metabolism*; D061307:Human Umbilical Vein Endothelial Cells; D006801:Humans; D008853:Microscopy / Q000379:methods*; D034881:Nuclear Lamina / Q000378:metabolism*; D011485:Protein Binding; D021381:Protein Transport; D022502:Stress Fibers / Q000378:metabolism
chemical_list: D002843:Chromatin