TDP-43 and FUS/TLS: sending a complex message about messenger RNA in amyotrophic lateral sclerosis?

FEBS J. 2011 Oct;278(19):3569-77. doi: 10.1111/j.1742-4658.2011.08277.x. Epub 2011 Sep 6.

Abstract

TAR DNA binding protein of 43 kDa (TDP-43) and fused in sarcoma/translocated in liposarcoma (FUS/TLS) have recently been linked to the pathology of amyotrophic lateral sclerosis (ALS). These proteins share many common features that include interaction with either DNA or RNA, participation in the formation of RNP complexes, the formation of pathological aggregates in degenerating motor neurons in ALS, and the ability to impact the RNA metabolism pathway at multiple levels from transcription to translation. Coupled with the observation that mutations in either TDP-43 or FUS/TLS are associated with ALS, this provides further support for the integral role of altered RNA metabolism in ALS.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amyotrophic Lateral Sclerosis / genetics*
  • Amyotrophic Lateral Sclerosis / pathology*
  • Amyotrophic Lateral Sclerosis / physiopathology
  • Animals
  • DNA / metabolism
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / metabolism*
  • Humans
  • Protein Structure, Tertiary
  • RNA, Messenger / metabolism*
  • RNA-Binding Protein FUS / chemistry
  • RNA-Binding Protein FUS / genetics
  • RNA-Binding Protein FUS / metabolism*

Substances

  • DNA-Binding Proteins
  • RNA, Messenger
  • RNA-Binding Protein FUS
  • DNA