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Abstract Lamins are nuclear intermediate filament proteins with diverse functions, ranging from organizing chromatin and regulating gene expression to providing structural support to the nucleus. Mammalian cells express two types of lamins, A-type and B-type, which, despite their similar structure and biochemical properties, exhibit distinct differences in expression, interaction partners, and function. One major difference is that A-type lamins have a significantly larger effect on the mechanical properties of the nucleus, which are crucial for protecting the nucleus from cytoskeletal forces, enabling cell migration through confined spaces, and contributing to cellular mechanotransduction. The molecular mechanism underlying this difference has remained unresolved. Here, we applied custom-developed biophysical and proteomic assays to lamin-deficient cell lines engineered to express specific full-length lamin proteins, lamin truncations, or chimeras combining domains from A- and B-type lamins, to systematically determine their contributions to nuclear mechanics. We found that although all expressed lamins contribute to the biophysical properties of the nuclear interior and confer some mechanical stability to the nuclear envelope, which is sufficient to protect the nuclear envelope from small cell-intrinsic forces and ensure proper positioning of nuclear pores, A-type lamins endow cells with a unique ability to resist large forces on the nucleus. Surprisingly, this effect was conferred through the A-type lamin rod domain, rather than the head or tail domains, which diverge more substantially between A- and B-type lamins and play important roles in lamin network formation. Collectively, our work provides an improved understanding of the distinct functions of different lamins in mammalian cells and may also explain why mutations in the A-type lamin rod domain cause more severe muscle defects in mouse models than other mutations. 

Brillouin spectrometers, used for characterizing material mechanical properties, traditionally employ etalons such as Fabry-Pérot interferometers and virtually imaged phased arrays (VIPA) that use spatial dispersion of the spectrum for measurement. Here, we introduce what we believe to be a novel approach to Brillouin spectroscopy using hot atomic vapors. Using laser induced circular dichroism of the rubidium D2 line in a ladder-type configuration, we developed a narrow-band monochromator for Brillouin analysis. Unlike etalon-based spectrometers, atomic line monochromators operate in free-space, facilitating Brillouin spectroscopy integration with microscopy instruments. We report the transmission and spectral resolution performances of the spectrometer and demonstrate Brillouin spectra measurements in liquids. 

Spectral imaging techniques extract spectral information using dispersive elements in combination with optical microscopes. For rapid acquisition, multiplexing spectral information along one dimension of imaged pixels has been demonstrated in hyperspectral imaging, as well as in Raman and Brillouin imaging. Full-field spectroscopy, i.e., multiplexing where imaged pixels are collected in 2D simultaneously while spectral analysis is performed sequentially, can increase spectral imaging speed, but so far has been attained at low spectral resolutions. Here, we extend 2D multiplexing to high spectral resolutions of ∼80 MHz (∼0.0001 nm) using high-throughput spectral discrimination based on atomic transitions.