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RNA quality control and protein aggregates in amyotrophic lateral sclerosis: A review
Author(s) -
Verma Ashok,
Tandan Rup
Publication year - 2013
Publication title -
muscle and nerve
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.025
H-Index - 145
eISSN - 1097-4598
pISSN - 0148-639X
DOI - 10.1002/mus.23673
Subject(s) - amyotrophic lateral sclerosis , motor neuron , neuroscience , rna , protein aggregation , biology , rna binding protein , gene , disease , genetics , medicine , pathology , spinal cord
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. Muscle Nerve 47:330‐338, 2013