Didier Hodzic

TL;DR: Data from this study support a model in which Sun proteins tether nesprins in the ONM via interactions spanning the PNS, and form a complex that links the nucleoskeleton and cytoskeleton (the LINC complex).

TL;DR: It is found that the shape of the nucleus is tightly regulated by the underlying cell adhesion geometry, and its nuclear shape-determining function is disrupted in cells from mouse models of accelerated aging and muscular dystrophy with distorted nuclei caused by alterations of A-type lamins.

TL;DR: Both the mechanical properties of the cytOSkeleton and cytoskeleton-based processes, including cell motility, coupled MTOC and nucleus dynamics, and cell polarization, depend critically on the integrity of the nuclear lamina, which suggest the existence of a functional mechanical connection between the nucleus and the cytos skeleton.

TL;DR: It is demonstrated that the disruption of endogenous LINC complexes affect cellular mechanical stiffness to an extent that compares to the loss of mechanical stiffness previously reported in embryonic fibroblasts derived from mouse lacking A-type lamins, a mouse model of muscular dystrophies and cardiomyopathies.

TL;DR: The structure and evolutionary conservation of SUN and KASH domain–containing proteins, whose interaction within the perinuclear space forms the “nuts and bolts” of LINC complexes, are reviewed and their function in nuclear, centrosomal, and chromosome dynamics, and their connection to human disease are discussed.