期刊
BIOCHEMICAL JOURNAL
卷 445, 期 -, 页码 93-100出版社
PORTLAND PRESS LTD
DOI: 10.1042/BJ20120304
关键词
cytoplasmic polyadenylation; mRNA translation; oocyte maturation; poly(A)-binding protein (PABP); phosphorylation; post-translational modification
资金
- National Institutes of Health [K08HD046581-01, R01HD059909]
- Medical Research Council (MRC) Unit [U1276.00.002.00011.01]
- MRC
- MRC [MC_U127692697, G117/564, MR/J003069/1] Funding Source: UKRI
- Medical Research Council [MC_U127692697, MR/J003069/1, G117/564] Funding Source: researchfish
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.
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