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J. Biol. Chem., Vol. 280, Issue 8, 6496-6503, February 25, 2005

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Proteomic Characterization of Messenger Ribonucleoprotein Complexes Bound to Nontranslated or Translated Poly(A) mRNAs in the Rat Cerebral Cortex^*

Frank Angenstein¶, Anne M. Evans||**, Shuo-Chien Ling, Robert E. Settlage||, Scott Ficarro||, Franklin A. Carrero-Martinez, Jeffrey Shabanowitz||, Donald F. Hunt||, and William T. Greenough

From the Beckman Institute/Neuronal Pattern Analysis, University of Illinois, Urbana, Illinois 61801, the ^||Department of Chemistry and the Department of Pathology, University of Virginia, Charlottesville, Virginia 22904, and ProteoMS, Limited Liability Corporation, Charlottesville, Virginia 22903

Receptor-triggered control of local postsynaptic protein synthesis plays a crucial role for enabling long lasting changes in synaptic functions, but signaling pathways that link receptor stimulation with translational control remain poorly known. Among the putative regulatory factors are mRNA-binding proteins (messenger ribonucleoprotein, mRNP), which control the fate of cytosolic localized mRNAs. Based on the assumption that a subset of mRNA is maintained in an inactive state, mRNP-mRNA complexes were separated into polysome-bound (translated) and polysome-free (nontranslated) fractions by sucrose density centrifugation. Poly(A) mRNA-mRNP complexes were purified from a postmitochondrial extract of rat cerebral cortex by oligo(dT)-cellulose affinity chromatography. The mRNA processing proteins were characterized, from solution, by a nanoflow reverse phase-high pressure liquid chromatography-µ-electrospray ionization mass spectrometry. The majority of detected mRNA-binding proteins was found in both fractions. However, a small number of proteins appeared to be fraction-specific. This subset of proteins is by far the most interesting because the proteins are potentially involved in controlling an activity-dependent onset of translation. They include transducer proteins, kinases, and anchor proteins. This study of the mRNP proteome is the first step in allowing future experimentation to characterize individual proteins responsible for mRNA processing and translation in dendrites.

Received for publication, November 10, 2004 , and in revised form, December 8, 2004.

^* This work was supported by the Fragile X Research Foundation (to F. A. and W. T. G) and National Institutes of Health Grant GM 37537 (to D. F. H.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Both authors contributed equally to this work.

^** Present address: Metabolon, Inc., Durham, NC 27713.

^¶ To whom correspondence should be addressed: Institute for Neurobiology, Brenneckestr. 6, 39120 Magdeburg, Germany. Tel.: 49-391-6263130; Fax: 49-391-6263328; E-mail: angenstein{at}ifn-magdeburg.de.

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