[Back to Issue 13 ToC] [Back to Journal Contents] [Back to Biochemistry (Moscow) Home page]
[View Full Article] [Download Reprint (PDF)]

REVIEW: Poly(A)-Binding Proteins: Structure, Domain Organization, and Activity Regulation


I. A. Eliseeva, D. N. Lyabin, and L. P. Ovchinnikov*

Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia; E-mail: yeliseeva@vega.protres.ru; lyabin@vega.protres.ru; ovchinn@vega.protres.ru

* To whom correspondence should be addressed.

Received May 6, 2013
RNA-binding proteins are of vital importance for mRNA functioning. Among these, poly(A)-binding proteins (PABPs) are of special interest due to their participation in virtually all mRNA-dependent events that is caused by their high affinity for A-rich mRNA sequences. Apart from mRNAs, PABPs interact with many proteins, thus promoting their involvement in cellular events. In the nucleus, PABPs play a role in polyadenylation, determine the length of the poly(A) tail, and may be involved in mRNA export. In the cytoplasm, they participate in regulation of translation initiation and either protect mRNAs from decay through binding to their poly(A) tails or stimulate this decay by promoting mRNA interactions with deadenylase complex proteins. This review presents modern notions of the role of PABPs in mRNA-dependent events; peculiarities of regulation of PABP amount in the cell and activities are also discussed.
KEY WORDS: PABPs, mRNA, translation, poly(A) tail, polyadenylation, mRNA decay

DOI: 10.1134/S0006297913130014