Abstract
The nuclear lamina is a major structural element of the nucleus, predominately
composed of the intermediate filament lamin proteins, enveloped by the nuclear
membrane. Underlining its importance to the mechanical and structural integrity of the nucleus, a persistent goal has been to examine the lamin network in situ. Here we apply an integrative approach combining techniques from
mechanobiology (atomic force microscopy), visual proteomics (cryo-electron
tomography) and network analysis (molecular dynamic simulations) to understand the design principle of the lamin network. A detailed analysis of the
mechanical failure under nano-Newton forces of the endogenous lamins of
Xenopus laevis oocytes revealed the lamin filaments to be strong, stiff and
tough, equivalent to natural silk and the synthetic polymer Kevlar. The combined approach is unique, and provides understanding of the structure-function of proteins involved in diseases from a materials science perspective, the underlying goal of ‘materiomics’
composed of the intermediate filament lamin proteins, enveloped by the nuclear
membrane. Underlining its importance to the mechanical and structural integrity of the nucleus, a persistent goal has been to examine the lamin network in situ. Here we apply an integrative approach combining techniques from
mechanobiology (atomic force microscopy), visual proteomics (cryo-electron
tomography) and network analysis (molecular dynamic simulations) to understand the design principle of the lamin network. A detailed analysis of the
mechanical failure under nano-Newton forces of the endogenous lamins of
Xenopus laevis oocytes revealed the lamin filaments to be strong, stiff and
tough, equivalent to natural silk and the synthetic polymer Kevlar. The combined approach is unique, and provides understanding of the structure-function of proteins involved in diseases from a materials science perspective, the underlying goal of ‘materiomics’
Original language | English |
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Pages (from-to) | 469a |
Journal | Biophysical Journal |
Volume | 112 |
Issue number | 3 |
DOIs | |
State | Published - Feb 2017 |