Matrix elasticity regulates lamin-A,C phosphorylation and turnover with feedback to actomyosin.

ABSTRACT: Tissue microenvironments are characterized not only in terms of chemical composition but also by collective properties such as stiffness, which influences the contractility of a cell, its adherent morphology, and even differentiation. The nucleoskeletal protein lamin-A,C increases with matrix stiffness, confers nuclear mechanical properties, and influences differentiation of mesenchymal stem cells (MSCs), whereas B-type lamins remain relatively constant. Here we show in single-cell analyses that matrix stiffness couples to myosin-II activity to promote lamin-A,C dephosphorylation at Ser22, which regulates turnover, lamina physical properties, and actomyosin expression. Lamin-A,C phosphorylation is low in interphase versus dividing cells, and its levels rise with states of nuclear rounding

SUBMITTER: Buxboim A 

PROVIDER: S-EPMC4373646 | biostudies-literature | 2014 Aug

REPOSITORIES: biostudies-literature