Filament assembly of the C. elegans lamin in the absence of helix 1A

Rebecca de Leeuw, Rafael Kronenberg-Tenga, Matthias Eibauer, Ohad Medalia

Research output: Contribution to journalArticlepeer-review

Abstract

Lamins are the major constituent of the nuclear lamina, a protein meshwork underlying the inner nuclear membrane. Nuclear lamins are type V intermediate filaments that assemble into ~3.5 nm thick filaments. To date, only the conditions for the in vitro assembly of Caenorhabditis elegans lamin (Ce-lamin) are known. Here, we investigated the assembly of Ce-lamin filaments by cryo-electron microscopy and tomography. We show that Ce-lamin is composed of ~3.5 nm protofilaments that further interact in vitro and are often seen as 6–8 nm thick filaments. We show that the assembly of lamin filaments is undisturbed by the removal of flexible domains, that is, the intrinsically unstructured head and tail domains. In contrast, much of the coiled-coil domains are scaffold elements that are essential for filament assembly. Moreover, our results suggest that Ce-lamin helix 1A has a minor scaffolding role but is important to the lateral assembly regulation of lamin protofilaments.

Original languageEnglish
Pages (from-to)49-57
Number of pages9
JournalNucleus
Volume13
Issue number1
DOIs
StatePublished - 1 Jan 2022
Externally publishedYes

Keywords

  • C. elegans
  • cryo-electron tomography
  • intermediate filaments
  • lamins

ASJC Scopus subject areas

  • Cell Biology

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