Pathogenic mutations in genes encoding nuclear envelope proteins and defective nucleocytoplasmic connections

Exp Biol Med (Maywood). 2019 Nov;244(15):1333-1344. doi: 10.1177/1535370219862243. Epub 2019 Jul 12.

Abstract

Mutations in genes encoding nuclear lamins and associated nuclear envelope proteins have been linked to a broad range of inherited diseases affecting different tissues and organs. These diseases are often referred to as laminopathies. Scientists have yet to elucidate exactly how pathogenic mutations leading to alteration of a nuclear envelope protein cause disease. Our relatively recent research has shown that pathogenic mutations in genes encoding nuclear envelope proteins lead to defective nucleocytoplasmic connections that disrupt proper functioning of the linker of nucleoskeleton and cytoskeleton complex in the establishment of cell polarity. These defects may explain, at least in part, pathogenic mechanisms underlying laminopathies.

Impact statement: Mutations in genes encoding nuclear lamins and associated nuclear envelope proteins have been linked to several diseases affecting different tissues and organs. The pathogenic mechanisms underlying these diseases, often called laminopathies, remain poorly understood. Increased knowledge of the functions of different nuclear envelope proteins and the interactions between them is crucial to elucidate these disease mechanisms. Our research has shown that pathogenic mutations in genes encoding nuclear envelope proteins lead to defective nucleocytoplasmic connections that disrupt proper functioning of the linker of nucleoskeleton and cytoskeleton (LINC) complex in the establishment of cell polarity. These defects may contribute to the pathogenesis of laminopathies and provide novel targets for therapeutics.

Keywords: Lamin; SUN protein; linker of nucleoskeleton and cytoskeleton complex complex; nesprin; nuclear envelope.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Animals
  • Cell Polarity / physiology*
  • Humans
  • Membrane Proteins / physiology
  • Mutation
  • Nuclear Envelope / physiology*
  • Nuclear Proteins / physiology*

Substances

  • Membrane Proteins
  • Nuclear Proteins