4.6 Article

DAZAP1 interacts via its RNA-recognition motifs with the C-termini of other RNA-binding proteins

Journal

Publisher

ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2009.01.166

Keywords

mRNA; AU-rich element; hnRNP; Translation; Protein-protein interaction

Funding

  1. UK Medical Research Council
  2. Royal Society
  3. Medical Research Council [MC_U127084348] Funding Source: researchfish
  4. MRC [MC_U127084348] Funding Source: UKRI

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The turnover and translation of many human mRNAs is regulated by AU-rich elements present in their 3'-untranslated region, which bind various trans acting factors. We previously identified a trans acting factor that interacts with these cis elements as DAZAP1 (deleted in Azoospermia (DAZ)-Associated Protein 1), whose interaction with the germ cell-specific protein DAZ was disrupted by the phosphorylation of DAZAP1. Here we have identified several other RNA-binding proteins as binding partners for DAZAP1 in non-germinal cells. Unlike DAZ, these interactions Occur between the RNA recognition motifs of DAZAP1 and the C-termini of the binding partners and in a phosphorylation-independent manner. The results suggest that DAZAP1 is a component of complexes that are crucial for the degradation and silencing of mRNA. (C) 2009 Elsevier Inc. All rights reserved.

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