Biochemical Properties and Biological Functions of FET Proteins

Members of the FET protein family, consisting of FUS, EWSR1, and TAF15, bind to RNA and contribute to the control of transcription, RNA processing, and the cytoplasmic fates of messenger RNAs in metazoa. FET proteins can also bind DNA, which may be important in transcription and DNA damage responses...

Full description

Saved in:
Bibliographic Details
Published in:Annual review of biochemistry 2015-06, Vol.84 (1), p.355-379
Main Authors: Schwartz, Jacob C, Cech, Thomas R, Parker, Roy R
Format: Article
Language:English
Subjects:
Active Transport, Cell Nucleus
Animals
Biochemistry
Biology
Cytoplasm
Dementia disorders
Deoxyribonucleic acid
DNA
DNA Repair
EWSR1
FUS
Genes
Humans
low-complexity
Neoplasms - metabolism
neurodegeneration
Neurodegenerative Diseases - metabolism
Pathogenesis
Proteins
RNA Processing, Post-Transcriptional
RNA-binding
RNA-Binding Protein FUS - chemistry
RNA-Binding Protein FUS - metabolism
RNA-Binding Proteins - chemistry
RNA-Binding Proteins - metabolism
TAF15
TATA-Binding Protein Associated Factors - chemistry
TATA-Binding Protein Associated Factors - metabolism
Transcription, Genetic
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Members of the FET protein family, consisting of FUS, EWSR1, and TAF15, bind to RNA and contribute to the control of transcription, RNA processing, and the cytoplasmic fates of messenger RNAs in metazoa. FET proteins can also bind DNA, which may be important in transcription and DNA damage responses. FET proteins are of medical interest because chromosomal rearrangements of their genes promote various sarcomas and because point mutations in FUS or TAF15 can cause neurodegenerative diseases such as amyotrophic lateral sclerosis and frontotemporal lobar dementia. Recent results suggest that both the normal and pathological effects of FET proteins are modulated by low-complexity or prion-like domains, which can form higher-order assemblies with novel interaction properties. Herein, we review FET proteins with an emphasis on how the biochemical properties of FET proteins may relate to their biological functions and to pathogenesis.
ISSN:0066-4154
1545-4509
DOI:10.1146/annurev-biochem-060614-034325