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A more recent version of this article appeared on August 1, 2006
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Submitted on October 12, 2005
Revised on May 15, 2006
Accepted on June 1, 2006
*Department of Neuroscience, Department of Molecular, Microbial, and Structural Biology, and Biomedical Science Graduate Program, University of Connecticut Health Center, Farmington, CT 06030
Monitoring Editor: Karsten Weis
Heterogeneous nuclear ribonucleoprotein (hnRNP) A2 is a trans-acting RNA-binding protein that mediates trafficking of RNAs containing the cis-acting A2 response element (A2RE). A2RE RNAs are transported to myelin in oligodendrocytes and to dendrites in neurons (Ainger et al., 1997; Shan et al., 2003). HnRNP E1 is an RNA-binding protein that regulates translation of specific mRNAs (Ostareck et al., 2001; Xiao et al., 2001). Here we show by yeast two-hybrid analysis, in vivo and in vitro coimmunoprecipitation, in vitro cross-linking, and fluorescence correlation spectroscopy that hnRNP E1 binds to hnRNP A2 and is recruited to A2RE RNA in an hnRNP A2-dependent manner. HnRNP E1 is colocalized with hnRNP A2 and A2RE mRNA in granules in dendrites of oligodendrocytes. Overexpression of hnRNP E1 or microinjection of exogenous hnRNP E1 in neural cells inhibits translation of A2RE mRNA, but not of nonA2RE RNA. Excess hnRNP E1 added to an in vitro translation system reduces translation efficiency of A2RE mRNA, but not of nonA2RE RNA, in an hnRNP A2-dependent manner. These results are consistent with a model where hnRNP E1 recruited to A2RE RNA granules by binding to hnRNP A2 inhibits translation of A2RE RNA during granule transport.
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