The adenosine-uridine binding factor recognizes the AU-rich elements of cytokine, lymphokine, and oncogene mRNAs.

Gillis, P.; Malter, James S.

doi:10.1016/s0021-9258(18)49970-x

Cited by 208 publications

(12 citation statements)

References 17 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Sequence analysis of the 3′ untranslated region (UTR) of ERG mRNAs often reveals adenosine-uridine-rich domains. These regions are often clustered into AUUUA repeats or AU-rich elements (AREs) which are widely accepted as mRNA instability determinants (9)(10)(11). Recent work suggests that the GUUUG repeats (2,12,13) or polyuridine stretches with interspersed purines (13)(14)(15)(16)) also exhibit destabilizing activity.…”

Section: Introductionmentioning

confidence: 99%

Identification of AUF-1 ligands reveals vast diversity of early response gene mRNAs

Bhattacharya

Giordano

Brewer

et al. 1999

Nucleic Acids Research

View full text Add to dashboard Cite

Cell activation is associated with diverse and widespread changes in gene expression at both the transcriptional and post-transcriptional levels. AUF1 is a recently described cytoplasmic protein which likely participates in the post-transcriptional regulation (PTR) of AU-rich (ARE) mRNAs including those coding for cytokines and proto-oncogenes. Individual mRNAs subject to AUF1-mediated PTR can be predicted if AREs are present or the mRNA in question interacts in vitro or in vivo with AUF1. However, there are few, if any, general approaches for characterizing the overall repertoire of mRNAs subject to PTR by AUF1. In an effort to identify these mRNAs, we incubated total mRNA from mitogen-activated peripheral blood mono-nuclear cells (PBMCs) with AUF1 in vitro. AUF1-mRNA complexes were retarded on membranes, bound mRNAs eluted with high salt, and either used to generate a cDNA library or rebound to AUF1 a second or third time prior to elution and cDNA library construction. We have obtained partial nucleotide sequences from 130 clones which shows that the AUF1 selected libraries are rich in mRNAs containing 3' untranslated region AREs including a large number of early response gene cDNAs. As a test of the validity of this method, we also show that a randomly selected, novel mRNA contained in the library is stabilized upon cell activation.

show abstract

Section: Introductionmentioning

confidence: 99%

Identification of AUF-1 ligands reveals vast diversity of early response gene mRNAs

Bhattacharya

Giordano

Brewer

et al. 1999

Nucleic Acids Research

View full text Add to dashboard Cite

show abstract

“…UV crosslinking of radiolabeled cytokine and proto-oncogene RNAs to cytoplasmic extracts of stimulated cells has identified multiple protein factors that may influence the decay of labile mRNAs (19)(20)(21). Indeed, there is substantial experimental support for activation of mRNA-binding proteins that specifically interact with RNase-sensitive sequences in the coding or 3′-untranslated regions (3′-UTRs) of labile cytokine or proto-oncogene mRNAs (16)(17)(18)(19)(20)(21)22). The ensuing transient resistence to cytoplasmic decay contributes to a 50-100-fold increase in protein production upon cell activation (23,24).…”

Section: Introductionmentioning

confidence: 99%

hnRNP C increases amyloid precursor protein (APP) production by stabilizing APP mRNA

Rajagopalan

Westmark

Jarzembowski

et al. 1998

Nucleic Acids Research

110

View full text Add to dashboard Cite

We have previously shown that heterogeneous nuclear ribonucleoprotein C (hnRNP C) and nucleolin bound specifically to a 29 nt sequence in the 3'-untranslated region of amyloid precursor protein (APP) mRNA. Upon activation of peripheral blood mononuclear cells, hnRNP C and nucleolin acquired APP mRNA binding activity, concurrent with APP mRNA stabilization. These data suggested that the regulated interaction of hnRNP C and nucleolin with APP mRNA controlled its stability. Here we have directly examined the role of the cis element and trans factors in the turnover and translation of APP mRNA in vitro . In a rabbit reticulocyte lysate (RRL) translation system, a mutant APP mRNA lacking the 29 nt element was 3-4-fold more stable and synthesized 2-4-fold more APP as wild-type APP mRNA. Therefore, the 29 nt element functioned as an APP mRNA destabilizer. RNA gel mobility shift assays with the RRL suggested the presence of endogenous nucleolin, but failed to show hnRNP C binding activity. However, wild-type APP mRNA was stabilized and coded for 6-fold more APP when translated in an RRL system supplemented with exogenous active hnRNP C. Control mRNAs lacking the 29 nt element were unaffected by hnRNP C supplementation. Therefore, occupancy of the 29 nt element by hnRNP C stabilized APP mRNA and enhanced its translation.

show abstract

“…Our own analysis of the 3' untranslated of the rat p52(PAI-l) cDNA (Zeheb and Gelehrter, 1988), using the mIlPustell ssubsequence similarity search program, has revealed three sites (at positions 1935, 1999, and 2610 relative to the translation start codon) of complete sequence identity to the instability-associated pentanucleotide sequence AUUUA, as well as nine and six additional sites of 80% homology corresponding to the sequences AUUU(N) and (N)UUUA, respectively. Interaction of the AU binding factor (AUBF) with multiple reiterations of AUUUA motifs may function as one possible mechanism to increase the half-lives of intrinsically unstable mRNAs (Gillis and Malter, 1991). Consistent with this is the finding that phorbol esters stabilize certain labile mRNAs concomitant with an increase in AUBF activity (Malter and Huong, 1991).…”

Section: Acknowledgmentsmentioning

confidence: 91%

Vibrational Modes of G-Actin

Tirion

ben‐Avraham

Holmes

1994

Advances in Experimental Medicine and Biology

View full text Add to dashboard Cite

show abstract

The adenosine-uridine binding factor recognizes the AU-rich elements of cytokine, lymphokine, and oncogene mRNAs.

Cited by 208 publications

References 17 publications

Identification of AUF-1 ligands reveals vast diversity of early response gene mRNAs

Identification of AUF-1 ligands reveals vast diversity of early response gene mRNAs

hnRNP C increases amyloid precursor protein (APP) production by stabilizing APP mRNA

Vibrational Modes of G-Actin

Contact Info

Product

Resources

About