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Poly(A)-binding proteins and mRNA localization: who rules the roost?
Author(s) -
Nicola K. Gray,
Lenka Hrabálková,
Jessica P. Scanlon,
Richard Smith
Publication year - 2015
Publication title -
biochemical society transactions
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.562
H-Index - 144
eISSN - 1470-8752
pISSN - 0300-5127
DOI - 10.1042/bst20150171
Subject(s) - cytoplasm , translation (biology) , rna binding protein , messenger rna , poly(a) binding protein , microbiology and biotechnology , rna , biology , p bodies , stress granule , nucleus , genetics , gene
RNA-binding proteins are often multifunctional, interact with a variety of protein partners and display complex localizations within cells. Mammalian cytoplasmic poly(A)-binding proteins (PABPs) are multifunctional RNA-binding proteins that regulate multiple aspects of mRNA translation and stability. Although predominantly diffusely cytoplasmic at steady state, they shuttle through the nucleus and can be localized to a variety of cytoplasmic foci, including those associated with mRNA storage and localized translation. Intriguingly, PABP sub-cellular distribution can alter dramatically in response to cellular stress or viral infection, becoming predominantly nuclear and/or being enriched in induced cytoplasmic foci. However, relatively little is known about the mechanisms that govern this distribution/relocalization and in many cases PABP functions within specific sites remain unclear. Here we discuss the emerging evidence with respect to these questions in mammals.

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