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Defective Human SRP Induces Protein Quality Control and Triggers Stress Response.

Elena B Tikhonova1, Sneider Alexander Gutierrez Guarnizo1, Morgana K Kellogg1

  • 1Department of Cell Biology and Biochemistry, Texas Tech University Health Sciences Center, Lubbock, TX 79430, USA.

Journal of Molecular Biology
|October 10, 2022
PubMed
Summary

The Regulation of Aberrant Protein Production (RAPP) pathway degrades mRNAs for proteins failing to bind partners. Depleting SRP54 activates RAPP, impacting secretory and membrane protein production.

Keywords:
protein synthesis and transportsecretory proteinssignal Recognition particlesignal sequencetranslational control

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • The Regulation of Aberrant Protein Production (RAPP) is a cellular mechanism for protein quality control.
  • RAPP degrades messenger RNAs (mRNAs) encoding nascent proteins that do not associate with their natural partners during ribosomal synthesis.
  • The precise molecular mechanisms, substrates, and specificity of RAPP remain largely uncharacterized.

Purpose of the Study:

  • To investigate the generality of the RAPP pathway across the entire transcriptome.
  • To elucidate the role of the Signal Recognition Particle (SRP) in RAPP.
  • To understand the downstream effects of SRP dysfunction on cellular protein quality control networks.

Main Methods:

  • Depletion of the human SRP54 protein subunit.
  • Transcriptome-wide expression analysis.
  • Analysis of chaperone network expression and ribosome-associated ubiquitination.

Main Results:

  • Depletion of SRP54 broadly activates the RAPP pathway.
  • Decreased expression of mRNAs encoding numerous secretory and membrane proteins was observed.
  • Significant upregulation of HSP70/40/90 chaperone networks and increased ribosome-associated ubiquitination occurred.

Conclusions:

  • The RAPP pathway operates at the whole transcriptome level.
  • SRP54 plays a critical role in regulating RAPP.
  • Defects in protein trafficking and quality control involve complex interplay between RAPP, chaperones, and ribosome modifications.