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Related Concept Videos

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Nuclear Protein Sorting

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Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
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Proteins targeted to the nucleus carry short stretches of amino acid sequences called the nuclear localization signal or NLS. Classical nuclear localization signals are of two types: monopartite and bipartite NLS. Monopartite classical NLS (cNLS) consists of a single cluster of 4-8 amino acids. Bipartite cNLS consists of two clusters of  2-3 amino acids and a 9-12 residue long proline-rich linker bridging the two clusters. Signal clusters are rich in positively charged amino acids such as...
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Identifying Heteroprotein Complexes in the Nuclear Envelope.

Jared Hennen1, Kwang-Ho Hur1, John Kohler1

  • 1School of Physics and Astronomy, University of Minnesota, Minneapolis, Minnesota.

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|December 17, 2019
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Researchers developed dual-color time-shifted mean-segmented Q (DC tsMSQ) analysis to study protein complexes within the nuclear envelope (NE). This new method successfully characterizes heteroprotein complexes, like the linker of the nucleoskeleton and cytoskeleton, in living cells.

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Area of Science:

  • Cell Biology
  • Biophysics
  • Molecular Imaging

Background:

  • The nuclear envelope (NE) is a double membrane critical for cellular processes.
  • Conventional fluorescence fluctuation spectroscopy is limited in NE studies due to membrane dynamics.
  • Previous time-shifted mean-segmented Q (tsMSQ) analysis addressed homo-oligomerization but not heterotypic interactions.

Purpose of the Study:

  • To develop a dual-color tsMSQ (DC tsMSQ) method for analyzing heteroprotein complexes in the NE.
  • To characterize the stoichiometry and interactions of NE protein complexes in living cells.
  • To investigate the assembly of the linker of the nucleoskeleton and cytoskeleton complex.

Main Methods:

  • Development of dual-color tsMSQ (DC tsMSQ) for analyzing proteins with two distinct fluorescent labels.
  • Application of DC tsMSQ to model systems to validate its accuracy in identifying heteroprotein complexes and stoichiometry.
  • Utilizing DC tsMSQ to study the in vivo assembly of the linker of the nucleoskeleton and cytoskeleton complex in the NE.

Main Results:

  • DC tsMSQ successfully identifies heteroprotein complexes and their stoichiometry in the NE.
  • The method accounts for spectral cross talk and local volume fluctuations.
  • Demonstrated the in vivo formation of a heterocomplex between SUN2 and nesprin-2 using DC tsMSQ.

Conclusions:

  • DC tsMSQ is a powerful technique for characterizing NE heteroprotein complexes.
  • The study validates the utility of DC tsMSQ for in vivo analysis of complex assembly.
  • Results support previous in vitro findings on the linker of the nucleoskeleton and cytoskeleton complex.