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- W2493857976 abstract "The importance of the nuclear envelope extends well beyond separating the cytoplasm and nucleoplasm. The perinuclear space (PS) located within the nuclear envelope contains proteins involved in many cellular functions including cellular signaling, force transduction, and mechanical properties of the cell. Protein oligomerization plays a central role in the control of these biological processes. Currently, there is no technique that allows for quantitative, real time exploration of the oligomeric state of proteins inside the PS. We previously used fluorescence fluctuation spectroscopy (FFS) with brightness analysis to measure the oligomeric state of protein complexes in the cytoplasm, the nucleus, and the plasma membrane. To extend these measurements to the PS we performed z-scan FFS to account for the layered structure of the nuclear envelope within the cell. However, the conventional analysis tools that allowed us to quantify protein complexes in the cytoplasm and at the plasma membrane failed in the PS. To overcome this obstacle we explored an alternative analysis approach and tested it on fluorescent proteins that were co-translationally targeted to the PS. We compared the recovered diffusion and brightness of these proteins in the PS and in the cytoplasm. We extended our investigation to functional proteins, including SUN2, and demonstrate that measurements of the oligomeric state of protein complexes in the PS are feasible. This work has been supported by a grant from the National Institutes of Health (R01 GM64589)." @default.
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- W2493857976 date "2016-02-01" @default.
- W2493857976 modified "2023-09-27" @default.
- W2493857976 title "Fluorescence Fluctuation Spectroscopy in the Perinuclear Space" @default.
- W2493857976 doi "https://doi.org/10.1016/j.bpj.2015.11.2636" @default.
- W2493857976 hasPublicationYear "2016" @default.
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