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Post-translational Translocation of Proteins to the RER

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Repressing Gene Transcription by Redirecting Cellular Machinery with Chemical Epigenetic Modifiers
10:28

Repressing Gene Transcription by Redirecting Cellular Machinery with Chemical Epigenetic Modifiers

Published on: September 20, 2018

Transient CPEB dimerization and translational control.

Chien-Ling Lin1, Yen-Tsung Huang, Joel D Richter

  • 1Program in Molecular Medicine, University of Massachusetts Medical School, Worcester, Massachusetts 01605, USA.

RNA (New York, N.Y.)
|March 30, 2012
PubMed
Summary
This summary is machine-generated.

Cytoplasmic polyadenylation element-binding protein (CPEB) forms inactive dimers to regulate mRNA polyadenylation during oocyte development. Dimer degradation controls the timing of translation, ensuring proper meiotic progression.

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Single-molecule Imaging of Gene Regulation In vivo Using Cotranslational Activation by Cleavage (CoTrAC)
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Single-molecule Imaging of Gene Regulation In vivo Using Cotranslational Activation by Cleavage (CoTrAC)
11:31

Single-molecule Imaging of Gene Regulation In vivo Using Cotranslational Activation by Cleavage (CoTrAC)

Published on: March 15, 2013

Area of Science:

  • Molecular Biology
  • Developmental Biology
  • Cell Biology

Background:

  • Cytoplasmic polyadenylation element-binding protein (CPEB) is crucial for mRNA polyadenylation and translation during oocyte development.
  • Regulation of CPEB activity involves phosphorylation, affecting its stability and the polyadenylation apparatus.
  • Precise control of CPEB and mRNA stoichiometry is essential for temporal mRNA polyadenylation during meiosis.

Purpose of the Study:

  • To investigate the hypothesis that excess CPEB is sequestered in an inactive form through dimerization.
  • To determine the role of CPEB dimerization in regulating polyadenylation and translation during oocyte maturation.
  • To elucidate the mechanisms by which CPEB dimers are regulated and their impact on the polyadenylation machinery.

Main Methods:

  • Demonstration of CPEB dimerization using biochemical assays.
  • Investigation of the role of RNA-binding domains in CPEB dimerization.
  • Analysis of CPEB dimer stability and degradation pathways involving plx1 and β-TrCP.
  • Assessment of the binding affinities of CPEB monomers and dimers to RNA and polyadenylation factors.

Main Results:

  • CPEB forms dimers, a process dependent on its RNA-binding domains.
  • Dimerization renders CPEB unable to bind RNA (UV cross-linking), creating an inactive pool.
  • CPEB dimers are rapidly degraded during oocyte maturation due to higher affinity for plx1 and β-TrCP.
  • Dimeric CPEB exhibits higher affinity for cytoplasmic polyadenylation factors, suggesting a reservoir function.

Conclusions:

  • CPEB dimerization serves as a mechanism to inactivate excess protein, preventing aberrant polyadenylation.
  • The balance between CPEB monomers and dimers regulates mRNA polyadenylation and translational control during meiosis.
  • CPEB dimers may act as molecular hubs, sequestering polyadenylation factors and releasing them upon dimer destruction for translational activation.