Literature DB >> 23424172

Poly(A) binding proteins: are they all created equal?

Dixie J Goss1, Frida Esther Kleiman.   

Abstract

The PABP family of proteins were originally thought of as a simple shield for the mRNA poly(A) tail. Years of research have shown that PABPs interact not only with the poly(A) tail, but also with specific sequences in the mRNA, having a general and specific role on the metabolism of different mRNAs. The complexity of PABPs function is increased by the interactions of PABPs with factors involved in different cellular functions. PABPs participate in all the metabolic pathways of the mRNA: polyadenylation/deadenylation, mRNA export, mRNA surveillance, translation, mRNA degradation, microRNA-associated regulation, and regulation of expression during development. In this review, we update information on the roles of PABPs and emerging data on the specific interactions of PABP homologs. Specific functions of individual members of PABPC family in development and viral infection are beginning to be elucidated. However, the interactions are complex and recent evidence for exchange of nuclear and cytoplasmic forms of the proteins, as well as post-translational modifications, emphasize the possibilities for fine-tuning the PABP metabolic network.
Copyright © 2012 John Wiley & Sons, Ltd.

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Year:  2012        PMID: 23424172      PMCID: PMC3580857          DOI: 10.1002/wrna.1151

Source DB:  PubMed          Journal:  Wiley Interdiscip Rev RNA        ISSN: 1757-7004            Impact factor:   9.957


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