| Literature DB >> 20573744 |
Katrin Schäffler1, Kristina Schulz, Anja Hirmer, Julia Wiesner, Michael Grimm, Albert Sickmann, Utz Fischer.
Abstract
La-related proteins (LARPs) belong to an evolutionarily conserved family of factors with predicted roles in RNA metabolism. Here, we have analyzed the cellular interactions and function of LARP4B, a thus far uncharacterized member of the LARP family. We show that LARP4B is a cytosolic protein that accumulates upon arsenite treatment in cellular stress granules. Biochemical experiments further uncovered an interaction of LARP4B with the cytosolic poly(A) binding protein 1 (PABPC1) and the receptor for activated C Kinase (RACK1), a component of the 40S ribosomal subunit. Under physiological conditions, LARP4B co-sedimented with polysomes in cellular extracts, suggesting a role in translation. In agreement with this notion, overexpression of LARP4B stimulated protein synthesis, whereas knockdown of the factor by RNA interference impaired translation of a large number of cellular mRNAs. In sum, we identified LARP4B as a stimulatory factor of translation. We speculate that LARP4B exerts its function by bridging mRNA factors of the 3' end with initiating ribosomes.Entities:
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Year: 2010 PMID: 20573744 PMCID: PMC2905749 DOI: 10.1261/rna.2146910
Source DB: PubMed Journal: RNA ISSN: 1355-8382 Impact factor: 4.942