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Biomolecular Concepts

Editor-in-Chief: Di Cera, Enrico


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CiteScore 2018: 3.35

SCImago Journal Rank (SJR) 2018: 1.475
Source Normalized Impact per Paper (SNIP) 2018: 0.825

ICV 2018: 124.31

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Online
ISSN
1868-503X
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Volume 2, Issue 5

Issues

Fragile X family members have important and non-overlapping functions

Claudia Winograd
  • Neuroscience Program and College of Medicine, University of Illinois, 601 S. Goodwin Avenue, Urbana–Champaign, IL 61801, USA
  • Other articles by this author:
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/ Stephanie Ceman
  • Department of Cell and Developmental Biology, University of Illinois, 601 S. Goodwin Avenue, Urbana–Champaign, IL 61801, USA
  • Neuroscience Program and College of Medicine, University of Illinois, 601 S. Goodwin Avenue, Urbana–Champaign, IL 61801, USA
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Published Online: 2011-08-13 | DOI: https://doi.org/10.1515/BMC.2011.033

Abstract

The fragile X family of genes encodes a small family of RNA binding proteins including FMRP, FXR1P and FXR2P that were identified in the 1990s. All three members are encoded by 17 exons and show alternative splicing at the 3′ ends of their respective transcripts. They share significant homology in the protein functional domains, including the Tudor domains, the nuclear localization sequence, a protein-protein interaction domain, the KH1 and KH2 domains and the nuclear export sequence. Fragile X family members are found throughout the animal kingdom, although all three members are not consistently present in species outside of mammals: only two family members are present in the avian species examined, Gallus gallus and Taeniopygia guttata, and in the frog Xenopus tropicalis. Although present in many tissues, the functions of the fragile X family members differ, which are particularly evident in knockout studies performed in animals. The fragile X family members play roles in normal neuronal function and in the case of FXR1, in muscle function.

Keywords: fragile X; FMR1; FXR1; FXR2; RNA binding proteins

About the article

Corresponding author


Received: 2011-04-27

Accepted: 2011-06-29

Published Online: 2011-08-13

Published in Print: 2011-10-01


Citation Information: BioMolecular Concepts, Volume 2, Issue 5, Pages 343–352, ISSN (Online) 1868-503X, ISSN (Print) 1868-5021, DOI: https://doi.org/10.1515/BMC.2011.033.

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