Identification of FUSE-binding proteins as interacting partners of TIA proteins
- Laboratoire de Chimie Biologique, Institut de Biologie et de Medecine Moleculaires, Universite Libre de Bruxelles, 6041 Gosselies (Belgium)
- Laboratoire d' Embryologie Moleculaire, Institut de Biologie et de Medecine Moleculaires, Universite Libre de Bruxelles, 6041 Gosselies (Belgium)
TIA-1 and TIAR are closely related RNA-binding proteins involved in several mechanisms of RNA metabolism, including alternative hnRNA splicing and mRNA translation regulation. In particular, TIA-1 represses tumor necrosis factor (TNF) mRNA translation by binding to the AU-rich element (ARE) present in the mRNA 3' untranslated region. Here, we demonstrate that TIA proteins interact with FUSE-binding proteins (FBPs) and that fbp genes are co-expressed with tia genes during Xenopus embryogenesis. FBPs participate in various steps of RNA processing and degradation. In Cos cells, FBPs co-localize with TIA proteins in the nucleus and migrate into TIA-enriched cytoplasmic granules upon oxidative stress. Overexpression of FBP2-KH3 RNA-binding domain fused to EGFP induces the specific sequestration of TIA proteins in cytoplasmic foci, thereby precluding their nuclear accumulation. In cytosolic RAW 264.7 macrophage extracts, FBPs are found associated in EMSA to the TIA-1/TNF-ARE complex. Together, our results indicate that TIA and FBP proteins may thus be relevant biological involved in common events of RNA metabolism occurring both in the nucleus and the cytoplasm.
- OSTI ID:
- 20798918
- Journal Information:
- Biochemical and Biophysical Research Communications, Vol. 343, Issue 1; Other Information: DOI: 10.1016/j.bbrc.2006.02.112; PII: S0006-291X(06)00416-5; Copyright (c) 2006 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
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