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XB-ART-45117
Biochem J July 1, 2012; 445 (1): 93-100.
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Embryonic poly(A)-binding protein (ePAB) phosphorylation is required for Xenopus oocyte maturation.

Friend K , Brook M , Bezirci FB , Sheets MD , Gray NK , Seli E .


Abstract
Oocyte maturation and early embryonic development require the cytoplasmic polyadenylation and concomitant translational activation of stored maternal mRNAs. ePAB [embryonic poly(A)-binding protein, also known as ePABP and PABPc1-like] is a multifunctional post-transcriptional regulator that binds to poly(A) tails. In the present study we find that ePAB is a dynamically modified phosphoprotein in Xenopus laevis oocytes and show by mutation that phosphorylation at a four residue cluster is required for oocyte maturation. We further demonstrate that these phosphorylations are critical for cytoplasmic polyadenylation, but not for ePAB''s inherent ability to promote translation. Our results provide the first insight into the role of post-translational modifications in regulating PABP protein activity in vivo.

PubMed ID: 22497250
PMC ID: PMC3955212
Article link: Biochem J
Grant support: [+]

Species referenced: Xenopus laevis
Genes referenced: pabpc1 pabpc1l pabpc4

References [+] :
Brook, The DAZL and PABP families: RNA-binding proteins with interrelated roles in translational control in oocytes. 2009, Pubmed, Xenbase