TAILIEUCHUNG - Báo cáo khoa học: Annexin A2 binds to the localization signal in the 3¢ untranslated region of c-myc mRNA

Messenger RNA trafficking, which provides a mechanism for local protein synthesis, is dependent on cis-acting sequences in the 3¢ untranslated regions (3¢UTRs) of the mRNAs concerned acting together withtrans-act-ing proteins. The C-MYC transcription factor is a proto-oncogene product involved in cell proliferation, differentiation and apoptosis. Localization of c-myc mRNA to the perinuclear cytoplasm and its association with the cytoskeleton is determined by a signal in the 3¢UTR. | ềFEBS Journal Annexin A2 binds to the localization signal in the 3 untranslated region of c-myc mRNA Ian Mickleburgh1 Brian Burtle1 Hanne Hollas2 Gill Campbell3 Zofia Chrzanowska-Lightowlers4 Anni Vedeler2 and John Hesketh1 1 Schoolof Celland Molecular Biosciences University of Newcastle UK 2 Department of Biomedicine University of Bergen Norway 3 Rowett Research Institute Aberdeen UK 4 Schoolof Neurology Neurobiology and Psychiatry University of Newcastle UK Keywords cytoskeleton mRNA localization RNA-binding protein targeting 3 UTR Correspondence J. Hesketh Schoolof Celland Molecular Biosciences University of Newcastle Newcastle-upon-Tyne NE1 7RU UK Fax 44 191 222 8684 Tel 44 191 222 8744 E-mail Received 1 September 2004 revised 20 October 2004 accepted 15 November 2004 doi Messenger RNA trafficking which provides a mechanism for local protein synthesis is dependent on cis-acting sequences in the 3 untranslated regions 3 UTRs of the mRNAs concerned acting together with trans-act-ing proteins. The C-MYC transcription factor is a proto-oncogene product involved in cell proliferation differentiation and apoptosis. Localization of c-myc mRNA to the perinuclear cytoplasm and its association with the cytoskeleton is determined by a signal in the 3 UTR. Here we show the specific binding of a trans-acting factor to the perinuclear localization element in the 3 UTR of c-myc mRNA and identify this protein as annexin A2. Gel retardation and UV cross-linking experiments showed that proteins in fibroblast extracts formed complexes with the region of c-myc 3 UTR implicated in localization a protein of w 36 kDa exhibited specific Ca2 -dependent binding. Binding was reduced by introduction of a mutation that abrogates localization. Using RNA-affinity columns followed by gel electrophoresis and mass spectrometry this protein was identified as annexin A2. The RNA-protein complex formed by cell extracts was further retarded by

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