LINCing complex functions at the nuclear envelope: what the molecular architecture of the LINC complex can reveal about its function

Nucleus. 2013 Jan-Feb;4(1):29-36. doi: 10.4161/nucl.23387. Epub 2013 Jan 1.

Abstract

Linker of nucleoskeleton and cytoskeleton (LINC) complexes span the double membrane of the nuclear envelope (NE) and physically connect nuclear structures to cytoskeletal elements. LINC complexes are envisioned as force transducers in the NE, which facilitate processes like nuclear anchorage and migration, or chromosome movements. The complexes are built from members of two evolutionary conserved families of transmembrane (TM) proteins, the SUN (Sad1/UNC-84) domain proteins in the inner nuclear membrane (INM) and the KASH (Klarsicht/ANC-1/SYNE homology) domain proteins in the outer nuclear membrane (ONM). In the lumen of the NE, the SUN and KASH domains engage in an intimate assembly to jointly form a NE bridge. Detailed insights into the molecular architecture and atomic structure of LINC complexes have recently revealed the molecular basis of nucleo-cytoskeletal coupling. They bear important implications for LINC complex function and suggest new potential and as yet unexplored roles, which the complexes may play in the cell.

Keywords: KASH domain; LINC complex; SUN domain; mechanotransduction; membrane fusion; nuclear envelope; nuclear membrane spacing; nuclear pore complex; spermatogenesis; spindle pole body.

MeSH terms

  • Cytoskeleton / metabolism*
  • Humans
  • Intracellular Signaling Peptides and Proteins / metabolism
  • Mechanotransduction, Cellular
  • Membrane Proteins / metabolism
  • Microtubule-Associated Proteins / metabolism
  • Nuclear Envelope / metabolism*
  • Nuclear Matrix / metabolism*
  • Nuclear Proteins / metabolism
  • Protein Serine-Threonine Kinases / metabolism
  • Protein Structure, Tertiary

Substances

  • Intracellular Signaling Peptides and Proteins
  • Membrane Proteins
  • Microtubule-Associated Proteins
  • Nuclear Proteins
  • SUN1 protein, human
  • BRSK1 protein, human
  • Protein Serine-Threonine Kinases