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Conserved SUN-KASH Interfaces Mediate LINC Complex-Dependent Nuclear Movement and Positioning.

Natalie E Cain1, Zeinab Jahed2, Amy Schoenhofen3

  • 1Department of Molecular and Cellular Biology, University of California, Davis, 1 Shields Avenue, Davis, CA 95616, USA.

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|September 25, 2018
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Summary

Linker of nucleoskeleton and cytoskeleton (LINC) complexes regulate nuclear positioning. This study reveals how SUN-KASH protein interactions, including disulfide bonds, control nuclear migration and anchorage, offering targets for regulation.

Keywords:
KASH proteinsLINC complexNesprinSUN proteinsnuclear envelopenuclear positioning

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biophysics

Background:

  • Nuclear positioning is crucial for cellular function and relies on Linker of Nucleoskeleton and Cytoskeleton (LINC) complexes.
  • LINC complexes mediate force transmission across the nuclear envelope via SUN and KASH protein interactions.
  • Regulation of these SUN-KASH interactions remains poorly understood.

Purpose of the Study:

  • To elucidate the regulatory mechanisms of LINC complex function in nuclear positioning.
  • To investigate the role of specific SUN-KASH binding interfaces, including disulfide bonds, in nuclear migration and anchorage.

Main Methods:

  • In vivo C. elegans genetics to study nuclear migration and anchorage.
  • In vitro studies of wounded fibroblast polarization.
  • In silico molecular dynamics simulations to analyze force transmission.

Main Results:

  • Mutations in C. elegans UNC-83 KASH domain blocked nuclear migration.
  • Analogous mutations in mouse nesprin-2 disrupted nuclear movements but not anchorage.
  • Conserved cysteines forming disulfide bonds are critical for LINC complex function, potentially mediating a switch between migration and anchorage.
  • Disulfide bonds are necessary for maximal force transmission by LINC complexes.

Conclusions:

  • SUN-KASH binding interfaces, particularly disulfide bonds, are key determinants of nuclear positioning.
  • These interactions regulate distinct processes of nuclear migration and anchorage.
  • The findings provide insights into potential regulatory targets for controlling nuclear positioning.