RNA quality control and protein aggregates in amyotrophic lateral sclerosis: A review

Ashok Verma, Rup Tandan

Research output: Contribution to journalReview article

17 Scopus citations

Abstract

Amyotrophic lateral sclerosis (ALS) is the most common motor neuron disease in adults. The biologic basis of ALS remains unknown. However, ALS research has taken a dramatic turn over the past 4 years. Ground breaking discoveries of mutations of genes that encode RNA processing proteins, and demonstration that abnormal aggregates of these and other proteins precede motor neuron loss in familial and sporadic ALS, have initiated a paradigm shift in understanding the pathogenic mechanisms of ALS. Curiously, some of these RNA binding proteins have prion-like domains, with a propensity to self-aggregation. The emerging hypothesis that a focal cascade of toxic protein aggregates, and their consequent non-cell-autonomous spread to neighborhood groups of neurons, fits the classical temporo-spatial progression of ALS. This article reviews the current research efforts toward understanding the role of RNA-processing regulation and protein aggregates in ALS.

Original languageEnglish (US)
Pages (from-to)330-338
Number of pages9
JournalMuscle and Nerve
Volume47
Issue number3
DOIs
StatePublished - Mar 1 2013

Keywords

  • ALS
  • FUS/TLS
  • Protein aggregates
  • RNA metabolism
  • TDP-43

ASJC Scopus subject areas

  • Clinical Neurology
  • Cellular and Molecular Neuroscience
  • Physiology (medical)
  • Physiology

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