Regulation of EDEN-dependent deadenylation of Aurora A/Eg2-derived mRNA via phosphorylation and dephosphorylation in Xenopus laevis egg extracts.
Deadenylation is an intimate part of the post-transcriptional regulation of maternal mRNAs in embryos. EDEN-BP is so far the only known member of a complex regulating the deadenylation of maternal mRNA in Xenopus laevis embryos in a manner that is dependent on the 3'-untranslated region called EDEN (embryo deadenylation element). In this report, we show that calcium activation of cell-free extracts triggers EDEN binding protein (EDEN-BP) dephosphorylation and concomitant deadenylation of a chimeric RNA bearing Aurora A/Eg2 EDEN sequence. Deadenylation of mRNA deprived of EDEN sequence (default deadenylation) does not change with egg activation. Kinase and phosphatase inhibitors downregulate EDEN-dependent deadenylation but they do not substantially influence default deadenylation. Using indestructible Delta90 cyclin B to revert interphase extracts to the M-phase, we show that modulation of EDEN-dependent deadenylation is independent of M-phase promoting factor (MPF) activity. These results suggest that the increase in EDEN-dependent deadenylation following egg activation is achieved, at least partially, via dephosphorylation and/or phosphorylation of regulatory proteins, including EDEN-BP dephosphorylation. This regulation proceeds in a manner independent from MPF inactivation.
UMR 6061 CNRS, University of Rennes 1, Faculty of Medicine, 2 Ave. Prof. Léon Bernard, CS 34317, 35043 Rennes Cedex, France.
Lenaick
L
Detivaud
Gaetan
G
Pascreau
Anthi
A
Karaiskou
Howard B
HB
Osborne
Jacek Z
JZ
Kubiak
D020413:3' Untranslated Regions / Q000235:genetics; D000249:Adenosine Monophosphate / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D064127:Aurora Kinases; D002118:Calcium / Q000737:chemistry / Q000494:pharmacology; D020013:Calcium Signaling / Q000187:drug effects / Q000235:genetics; D018797:Cell Cycle Proteins; D002457:Cell Extracts / Q000737:chemistry; D002474:Cell-Free System / Q000737:chemistry / Q000378:metabolism; D019926:Cyclin B / Q000235:genetics; D004791:Enzyme Inhibitors / Q000494:pharmacology; D005260:Female; D005809:Genes, Regulator / Q000235:genetics; D016200:Maturation-Promoting Factor / Q000235:genetics / Q000378:metabolism; D009865:Oocytes / Q000737:chemistry / Q000378:metabolism*; D010766:Phosphorylation / Q000187:drug effects; D011494:Protein Kinases / Q000235:genetics*; D017346:Protein Serine-Threonine Kinases; D012323:RNA Processing, Post-Transcriptional / Q000502:physiology; D023121:RNA, Messenger, Stored / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000187:drug effects / Q000235:genetics / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000235:genetics; D029867:Xenopus Proteins / Q000187:drug effects / Q000235:genetics / Q000378:metabolism*; D014982:Xenopus laevis
D020413:3' Untranslated Regions; D018797:Cell Cycle Proteins; D002457:Cell Extracts; D019926:Cyclin B; C110462:EDEN-specific RNA-binding protein, Xenopus; D004791:Enzyme Inhibitors; D023121:RNA, Messenger, Stored; D016601:RNA-Binding Proteins; D011993:Recombinant Fusion Proteins; D029867:Xenopus Proteins; D000249:Adenosine Monophosphate; D011494:Protein Kinases; C112134:AURKA protein, Xenopus; D064127:Aurora Kinases; D017346:Protein Serine-Threonine Kinases; D016200:Maturation-Promoting Factor; D002118:Calcium