Ubiquitin ligases and a processive proteasome facilitate protein clearance during the oocyte-To-embryo transition in Caenorhabditis elegans

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4 Scopus citations


The ubiquitin-mediated degradation of oocyte translational regulatory proteins is a conserved feature of the oocyte-To-embryo transition. In the nematode Caenorhabditis elegans, multiple translational regulatory proteins, including the TRIM-NHL RNA-binding protein LIN-41/Trim71 and the Pumilio-family RNA-binding proteins PUF-3 and PUF-11, are degraded during the oocyte-To-embryo transition. Degradation of each protein requires activation of the M-phase cyclin-dependent kinase CDK-1, is largely complete by the end of the first meiotic division and does not require the anaphase-promoting complex. However, only LIN-41 degradation requires the F-box protein SEL-10/FBW7/Cdc4p, the substrate recognition subunit of an SCF-Type E3 ubiquitin ligase. This finding suggests that PUF-3 and PUF-11, which localize to LIN-41-containing ribonucleoprotein particles, are independently degraded through the action of other factors and that the oocyte ribonucleoprotein particles are disassembled in a concerted fashion during the oocyte-To-embryo transition. We develop and test the hypothesis that PUF-3 and PUF-11 are targeted for degradation by the proteasome-Associated HECT-Type ubiquitin ligase ETC-1/UBE3C/Hul5, which is broadly expressed in C. elegans. We find that several GFP-Tagged fusion proteins that are degraded during the oocyte-To-embryo transition, including fusions with PUF-3, PUF-11, LIN-41, IFY-1/Securin, and CYB-1/Cyclin B, are incompletely degraded when ETC-1 function is compromised. However, it is the fused GFP moiety that appears to be the critical determinant of this proteolysis defect. These findings are consistent with a conserved role for ETC-1 in promoting proteasome processivity and suggest that proteasomal processivity is an important element of the oocyte-To-embryo transition during which many key oocyte regulatory proteins are rapidly targeted for degradation.

Original languageEnglish (US)
Article numberiyac051
Issue number1
StatePublished - May 2022

Bibliographical note

Publisher Copyright:
© The Author(s) 2022. Published by Oxford University Press on behalf of Genetics Society of America. All rights reserved. For permissions, please email: journals.permissions@oup.com.


  • RNA-binding proteins
  • oocyte meiotic maturation
  • oocyte-To-embryo transition
  • translational regulation
  • ubiquitin-mediated protein degradation

PubMed: MeSH publication types

  • Journal Article
  • Research Support, N.I.H., Extramural


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