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Vol. 16, Issue 9, 4350-4361, September 2005

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The RNA-binding Protein Fragile X-related 1 Regulates Somite Formation in Xenopus laevis

Marc-Etienne Huot ^*  , Nicolas Bisson  , Laetitia Davidovic ^* , Rachid Mazroui ^||, Yves Labelle ^* , Tom Moss  , and Edouard W. Khandjian ^* 

^* Unité de recherche en génétique humaine et moléculaire, CHUQ-St-François d'Assise, Québec, Québec G1L 3L5, Canada; Centre de recherche en cancérologie de l'Université Laval, CHUQ-Hôtel-Dieu de Québec, Québec, Québec G1R 2J6, Canada; Département de Biologie Médicale, Faculté de Médecine, Université Laval, Québec, Québec G1V 4G2, Canada; and ^|| Department of Biochemistry, McGill University, Montréal, Québec H3A 2K6, Canada

Submitted April 11, 2005; Revised June 13, 2005; Accepted June 28, 2005
Monitoring Editor: Marvin P. Wickens

Fragile X-related 1 protein (FXR1P) is a member of a small family of RNA-binding proteins that includes the Fragile X mental retardation 1 protein (FMR1P) and the Fragile X-related 2 protein (FXR2P). These proteins are thought to transport mRNA and to control their translation. While FMR1P is highly expressed in neurons, substantial levels of FXR1P are found in striated muscles and heart, which are devoid of FMRP and FXR2P. However, little is known about the functions of FXR1P. We have isolated cDNAs for Xenopus Fxr1 and found that two specific splice variants are conserved in evolution. Knockdown of xFxr1p in Xenopus had highly muscle-specific effects, normal MyoD expression being disrupted, somitic myotomal cell rotation and segmentation being inhibited, and dermatome formation being abnormal. Consistent with the absence of the long muscle-specific xFxr1p isoform during early somite formation, these effects could be rescued by both the long and short mRNA variants. Microarray analyses showed that xFxr1p depletion affected the expression of 129 known genes of which 50% were implicated in muscle and nervous system formation. These studies shed significant new light on Fxr1p function(s).

The online version of this article contains supplemental material at MBC Online (http://www.molbiolcell.org).

Present address: Lady Davis Institute for Medical Research, McGill University, Montréal, Québec H3A 2A7, Canada.

Address correspondence to: Edouard W. Khandjian (edward.khandjian{at}crsfa.ulaval.ca).

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