Defining the RGG/RG motif

Thandapani, Palaniraja, O'Connor, Timothy R., Bailey, Timothy L. and Richard, Stephane (2013) Defining the RGG/RG motif. Molecular Cell, 50 5: 613-623. doi:10.1016/j.molcel.2013.05.021

Author Thandapani, Palaniraja
O'Connor, Timothy R.
Bailey, Timothy L.
Richard, Stephane
Title Defining the RGG/RG motif
Journal name Molecular Cell   Check publisher's open access policy
ISSN 1097-2765
Publication date 2013-06
Sub-type Critical review of research, literature review, critical commentary
DOI 10.1016/j.molcel.2013.05.021
Open Access Status
Volume 50
Issue 5
Start page 613
End page 623
Total pages 11
Place of publication Cambridge, MA, United States
Publisher Cell Press
Collection year 2014
Language eng
Abstract Motifs rich in arginines and glycines were recognized several decades ago to play functional roles and were termed glycine-arginine-rich (GAR) domains and/or RGG boxes. We review here the evolving functions of the RGG box along with several sequence variations that we collectively term the RGG/RG motif. Greater than 1,000 human proteins harbor the RGG/RG motif, and these proteins influence numerous physiological processes such as transcription, pre-mRNA splicing, DNA damage signaling, mRNA translation, and the regulation of apoptosis. In particular, we discuss the role of the RGG/RG motif in mediating nucleic acid and protein interactions, a function that is often regulated by arginine methylation and partner-binding proteins. The physiological relevance of the RGG/RG motif is highlighted by its association with several diseases including neurological and neuromuscular diseases and cancer. Herein, we discuss the evidence for the emerging diverse functionality of this important motif.
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Critical review of research, literature review, critical commentary
Collections: Official 2014 Collection
Institute for Molecular Bioscience - Publications
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