The cis- acting response element, A2RE, which is sufficient for cytoplasmic mRNA trafficking in oligodendrocytes, binds a small group of rat brain proteins. Predominant among these is heterogeneous nuclear ribonucleoprotein (hnRNP) A2, a trans-acting factor for cytoplasmic trafficking of RNAs bearing A2RE-like sequences. We have now identified the other A2RE-binding proteins as hnRNP A1/A1B, hnRNP B1, and four isoforms of hnRNP A3. The rat and human hnRNP A3 cDNAs have been sequenced, revealing the existence of alternatively spliced mRNAs. In Western blotting, 38-, 39-, 41-, and 41.5-kDa components were all recognized by antibodies against a peptide in the glycine-rich region of hnRNP A3, but only the 41- and 41.5-kDa bands bound antibodies to a 15-residue N-terminal peptide encoded by an alternatively spliced part of exon 1. The identities of these four proteins were verified by Edman sequencing and mass spectral analysis of tryptic fragments generated from electrophoretically separated bands. Sequence-specific binding of bacterially expressed hnRNP A3 to A2RE has been demonstrated by biosensor and UV cross-linking electrophoretic mobility shift assays. Mutational analysis and confocal microscopy data support the hypothesis that the hnRNP A3 isoforms have a role in cytoplasmic trafficking of RNA. The cis- acting response element, A2RE, which is sufficient for cytoplasmic mRNA trafficking in oligodendrocytes, binds a small group of rat brain proteins. Predominant among these is heterogeneous nuclear ribonucleoprotein (hnRNP) A2, a trans-acting factor for cytoplasmic trafficking of RNAs bearing A2RE-like sequences. We have now identified the other A2RE-binding proteins as hnRNP A1/A1B, hnRNP B1, and four isoforms of hnRNP A3. The rat and human hnRNP A3 cDNAs have been sequenced, revealing the existence of alternatively spliced mRNAs. In Western blotting, 38-, 39-, 41-, and 41.5-kDa components were all recognized by antibodies against a peptide in the glycine-rich region of hnRNP A3, but only the 41- and 41.5-kDa bands bound antibodies to a 15-residue N-terminal peptide encoded by an alternatively spliced part of exon 1. The identities of these four proteins were verified by Edman sequencing and mass spectral analysis of tryptic fragments generated from electrophoretically separated bands. Sequence-specific binding of bacterially expressed hnRNP A3 to A2RE has been demonstrated by biosensor and UV cross-linking electrophoretic mobility shift assays. Mutational analysis and confocal microscopy data support the hypothesis that the hnRNP A3 isoforms have a role in cytoplasmic trafficking of RNA. Establishment of asymmetry in cells requires selective localization of proteins. This may be accomplished by directed protein transport, a well established pathway for plasma membrane and secreted proteins, or by trafficking and subsequent localization of mRNA. Localization of RNA has been intensively studied in Drosophila and Xenopus oocytes (for reviews see Refs. 1Ding D. Lipshitz H.D. BioEssays. 1993; 15: 651-658Crossref PubMed Scopus (97) Google Scholar, 2Pokrywka N.J. Curr. Topics Dev. Biol. 1995; 31: 139-166Crossref PubMed Google Scholar, 3Lasko P. FASEB J. 1999; 13: 421-433Crossref PubMed Scopus (66) Google Scholar, 4Mowry K.L. Cote C.A. FASEB J. 1999; 13: 435-445Crossref PubMed Scopus (97) Google Scholar, 5Grunert S. St. Johnston D. Curr. Opin. Genet. Dev. 1996; 6: 395-402Crossref PubMed Scopus (64) Google Scholar, 6St Johnston D. Cell. 1995; 81: 161-170Abstract Full Text PDF PubMed Scopus (510) Google Scholar) and more recently in mammalian somatic cells (7Mohr E. Prog. 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Smith 1998; PubMed Scopus Google a of nuclear that to nascent and in of RNA have a close binding to hnRNP A2 and the to support cytoplasmic RNA trafficking in G.J. Carson J.H. Barbarese L. Smith Smith J. Biol. 1999; Full Text Full Text PDF PubMed Scopus Google Scholar). experiments have support to the that hnRNP A2 is in and the has been the hnRNP A2 response hnRNP A2 of mRNA the A2RE S. Barbarese E. Carson J.H. J. 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A. 2000; PubMed Scopus Google Scholar) but has been only at the cDNA against the and ends of human brain ribonucleoprotein were from and were to the ends of the to of the into an The were and and in rat brain from a of RNA isolated from of The in of RNA and were and by for rat or for human of RNA used in and Subsequent were the for and for of in an for used for of the and and and were used for the in were into and into E. bearing an were the were and the were and and for sequencing in and from The were Res. PubMed Scopus Google Scholar) to and protein and the at were used for of the E. A. K.L. Scholar). were against to of the human B1, and and were and to into The antibodies were isolated from by the at Edman sequencing of the A2RE-binding proteins were that were were generated by of bands from and the of in S. J. 2000; Google Scholar). The were by a and a gradient of in at and a spectral analysis an an to a The were separated a the of which the and the mass The proteins were identified by of the tryptic peptide from the sequences. of the hnRNP A3 fragments of the at of the were rat hnRNP A3 and into The verified by sequencing into which been to a in of an the and hnRNP A3. This used to E. cells that were to an of The cell were and the a or and The protein from the by the to and by proteins the and an at the were generated by were identified by mass an biosensor used to the for the of hnRNP A3 A2RE, used as a to binding from hnRNP A3 to the of a biosensor a D. in Scholar). the biosensor hnRNP A3 to the and the response protein by of at at been The to the and to the proteins were as and protein were in binding and and for The were then of in a UV The were or A2RE-binding rat brain proteins were isolated bearing A2RE or as G.J. Carson J.H. Smith 1998; PubMed Scopus Google Scholar). bound to the were by for at in or in and or used for mass from in in in and by The cells were at of to cell and and the cells were at in The other were from rat brain were in then for in in the cells were by for in in the and then in in for of A2 and A3, the cells were for at in the against hnRNP A3 and to hnRNP in for in and for and an to the cells were or confocal and in were RNA and or the in the region the protein and the segment the G.J. Carson J.H. Barbarese L. Smith Smith J. Biol. 1999; Full Text Full Text PDF PubMed Scopus Google Scholar). The cells were a to a the cells were at for to transport to the cells were for in and for in experiments G.J. Carson J.H. Smith 1998; PubMed Scopus Google Scholar, G.J. Carson J.H. Barbarese L. Smith Smith J. 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The of and for other that these be for the a verified by sequencing of the rat in these were from cDNA from human brain RNA. and the a expressed as a A. T. A. 2000; PubMed Scopus Google Scholar) The from that for the human S. T. T. A. K. Y. Cell Genet. 1993; PubMed Scopus Google Scholar) only by a of the in for at the of the RNA of cDNAs at the and of at the the these human the that the proteins from but subsequent of the human data that the of these cDNAs to from of a The human cDNA from the rat from in the and by the of a in the but these only in of a the of the rat that these proteins cDNA to by and and rat brain RNA an that a in the of a of rat which a but region and a the of the region This to a mass of in the The and experiments that the human and rat in the to the used in the amplification of the rat The of the and cDNAs to for proteins from and Res. 1993; 21: PubMed Scopus Google Scholar). hnRNP a nuclear localization that is to be for the and G. J. 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The peptide which used in experiments is in the N-terminal alternatively spliced The is in a segment of the glycine-rich region to be to all of A3 but in and In Western the recognized the 41- and 41.5-kDa that only these proteins the segment encoded exon the all four 38-, 39-, 41-, and 41.5-kDa as hnRNP proteins and isoforms of or This by Edman sequencing and mass from were and and the were to Edman The in the of of these proteins as hnRNP A3. of the tryptic of the bands to liquid chromatography-mass and the peptide were from the protein sequences. fragments or more of the translated cDNA the of tryptic fragments of hnRNP A3 the protein the to the and the the of which a at a mass to a peptide for The protein in the tryptic and the of in the mass spectral that protein is expressed at hnRNP A3. all four bands to be alternatively spliced of hnRNP A3, of the the of exon 1. spliced of and A2 the or of exon in and M. F. A. G. S. 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T. 2000; PubMed Scopus Google Scholar). that the four of A3 from or of alternatively spliced from Edman the the for the 41.5-kDa in in the of the and were in the and and in the the of and The in and A2 that from in and and from the A2RE-binding proteins were isolated by and to Edman the the for the 41.5-kDa in in the of the and were in the and and in the the of and The in and A2 that from in and in a 38-, 39-, 41-, and 41.5-kDa A2RE-binding proteins all isoforms of hnRNP in in in in that only in rat hnRNP A3 and in the protein encoded by the that only in rat hnRNP A3 and in the protein encoded by the that only in rat hnRNP A3 and in the protein encoded by the that only in rat hnRNP A3 and in the protein encoded by the that only in rat hnRNP A3 and in the protein encoded by the that only in rat hnRNP A3 and in the protein encoded by the that only in rat hnRNP A3 and in the protein encoded by the that only in rat hnRNP A3 and in the protein encoded by the that only in rat hnRNP A3 and in the protein encoded by the in hnRNP A3 but the that only in rat hnRNP A3 and in the protein encoded by the in hnRNP A3 but the that only in rat hnRNP A3 and in the protein encoded by the that only in rat hnRNP A3 and in the protein encoded by the that only in rat hnRNP A3 and in the protein encoded by the that only in rat hnRNP A3 and in the protein encoded by the that only in rat hnRNP A3 and in the protein encoded by the that only in rat hnRNP A3 and in the protein encoded by the that only in rat hnRNP A3 and in the protein encoded by the that only in rat hnRNP A3 and in the protein encoded by the that only in rat hnRNP A3 and in the protein encoded by the by by by by that only in rat hnRNP A3 and in the protein encoded by the that only in rat hnRNP A3 and in the protein encoded by the that only in rat hnRNP A3 and in the protein encoded by the from of the bands were separated by and the by mass The from the and bands of hnRNP A3 and from the 41- and 41.5-kDa bands of hnRNP A3. The and as that only in rat hnRNP A3 and in the protein encoded by the in hnRNP A3 but the by in a from the A2RE-binding proteins were isolated by and to Edman from of the bands were separated by and the by mass The from the and bands of hnRNP A3 and from the 41- and 41.5-kDa bands of hnRNP A3. The and as A2RE-binding proteins were isolated experiments and to experiments and that the hnRNP A3 isoforms of hnRNP The a but only proteins were in the hnRNP A3 of and these the from the protein from the that the proteins have The in mass these to the mass of the segment encoded by the N-terminal the for of these and as the and isoforms and The and 41.5-kDa isoforms were in the mass and the and the other isoforms is in the mass and which close to the hnRNP A3 bands the A2RE as the hnRNP experiments A2RE have hnRNP A2 and the hnRNP that A2 binds the A2RE, that hnRNP A3 isolated hnRNP A2 a the as G.J. Carson J.H. Smith 1998; PubMed Scopus Google Scholar). We used the expressed hnRNP A3 in UV cross-linking electrophoretic mobility shift and biosensor rat hnRNP A3 expressed in E. as a protein and hnRNP A3 N-terminal from the of the protein by at a an the in that from the of the The hnRNP A3 the the A2RE-binding rat brain proteins an that rat protein in to the expressed This is the Western that the 41- and 41.5-kDa proteins the N-terminal in in which A2RE or to expressed hnRNP A3 the that the binding to protein the binding to hnRNP A2 J. K. G.J. Smith J. Biol. 2000; Full Text Full Text PDF PubMed Scopus Google Scholar). of or A2RE to the in a response A2RE that of sufficient A2RE to biosensor to This to in the response to A2RE but to a of the biosensor response of A2RE to the only of the of in the the biosensor response The the binding to A3 and A2 that the that binds RNA and a that support for from of the of This the binding of A2RE to hnRNP A3 and binding The of hnRNP A3 for and A2RE, as in the from the binding is for human hnRNP The for the is for hnRNP A2, and the for the and for hnRNP A3 and for hnRNP UV cross-linking electrophoretic mobility shift experiments binding of A2RE to A2 and A3 and binding of in the biosensor experiments the of the mobility shift UV cross-linking electrophoretic mobility shift experiments binding of A2 and hnRNP A3 to and an the of The of proteins, in the a of but of for the A2RE binding hnRNP A3. of or binding of to hnRNP experiments a hnRNP A2 binding to A2RE and and the of these to support transport of RNAs G.J. Carson J.H. Barbarese L. Smith Smith J. Biol. 1999; Full Text Full Text PDF PubMed Scopus Google Scholar). these a role for hnRNP A2 in cytoplasmic mRNA the binding to A2RE of hnRNP A3 that of A2 in these that the proteins may part in RNA but of requires a more The of hnRNP A3 has been of protein from rat were separated of an and for antibodies to A2 and the N-terminal peptide of A3. hnRNP A3 in in and and in these of hnRNP A2 or hnRNP A2 or A3 in or mass of proteins were in of hnRNP A3 is in cytoplasmic RNA be to be in cytoplasmic granules and to be RNA. microscopy hnRNP A3 to be in the and in cytoplasmic granules in the of A2 and A3 to of granules RNA hnRNP A3 in a of cytoplasmic granules data G.J. Carson J.H. Barbarese L. Smith Smith J. Biol. 1999; Full Text Full Text PDF PubMed Scopus Google Scholar) that in the A2RE that binding to hnRNP A2 and A3 RNA T. P. E. J. and that A2 and A3 a role in RNA trafficking in A2RE RNA and hnRNP A3 in were A2RE RNA. The of the RNA and hnRNP A3 were and by confocal and to hnRNP A3 the In the granules that A2RE RNA and hnRNP A3, and the granules only hnRNP A3 for hnRNP A3 but for RNA may transport RNA. analysis of hnRNP A3 and RNA in a the of the proteins and a of granules that hnRNP A3 but of RNA. RNA the A2RE is into the of G.J. Carson J.H. Barbarese L. Smith Smith J. Biol. 1999; Full Text Full Text PDF PubMed Scopus Google Scholar) or The four of the A2RE-binding rat brain proteins hnRNP A2 have been identified by mass and Edman sequencing of tryptic as hnRNP A3 isoforms and hnRNP A3 cDNA and the that of the four proteins were of or This the of Western antibodies against from hnRNP A3 In the of these proteins, the of human and rat hnRNP A3 The hnRNP A3 is and as of and human cDNAs were to hnRNP proteins, in protein the expressed and the other the hnRNP A3 A. T. 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Biol. 2000; Full Text Full Text PDF PubMed Scopus Google that hnRNP A3, hnRNP A2, of is binding to A2RE, and the other binds sequences. the RNA of hnRNP A3 in to hnRNP to hnRNP A2, hnRNP A3 hnRNP A2 more hnRNP in binding to A2RE, for A2RE binding that for hnRNP hnRNP A3 as a of the identified in cell is in isoforms in these cells A. A. E. N. A. J. 1996; PubMed Scopus Google Scholar). We have that hnRNP A3 is in the of hnRNP hnRNP A3, hnRNP A2, is in the of and and has a localization in other cell of hnRNP A3 A2RE in is by of in protein is to granules in that in and to to in trafficking of granules in the were for hnRNP A2 or hnRNP A3, but has been that in transport granules requires a hnRNP A2 and RNA and that of RNA and of hnRNP A2 in and J. that cytoplasmic granules A2 and A3 that these proteins other in RNA to the transport The that hnRNP A3 in the cytoplasmic trafficking of RNA is the of A2RE RNA hnRNP A3 in granules that the The in A2RE and of A2 and A3 the of these proteins the or in in RNA hnRNP A2 has been to be in cytoplasmic trafficking G.J. Carson J.H. Smith 1998; PubMed Scopus Google Scholar, G.J. Carson J.H. Barbarese L. Smith Smith J. Biol. 1999; Full Text Full Text PDF PubMed Scopus Google Scholar) and in the of S. Barbarese E. Carson J.H. J. 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