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Related Concept Videos

Yeast Signaling01:28

Yeast Signaling

Yeasts are single-celled organisms, but unlike bacteria, they are eukaryotes (cells with a nucleus). Cell signaling in yeast is similar to signaling in other eukaryotic cells. A ligand, such as a protein or a small molecule released from a yeast cell, attaches to a receptor on the cell surface. The binding stimulates second-messenger kinases to activate or inactivate transcription factors that further regulate gene expression. Many of the yeast intracellular signaling cascades have similar...
Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...

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Related Experiment Video

Updated: Jun 15, 2026

Applications of pHluorin for Quantitative, Kinetic and High-throughput Analysis of Endocytosis in Budding Yeast
10:02

Applications of pHluorin for Quantitative, Kinetic and High-throughput Analysis of Endocytosis in Budding Yeast

Published on: October 23, 2016

ERAD substrate recognition in budding yeast.

Wei Xie1, Davis T W Ng

  • 1Temasek Life Sciences Laboratory and Department of Biological Sciences, National University of Singapore, 1 Research Link, Singapore 117604, Singapore.

Seminars in Cell & Developmental Biology
|February 25, 2010
PubMed
Summary
This summary is machine-generated.

Cellular protein quality control identifies aberrant proteins not by misfolding, but by detecting those delayed in their maturation pathways via endoplasmic reticulum-associated degradation (ERAD). This ensures cellular viability by degrading unfolded proteins. Keywords: protein quality control, ERAD, cellular viability, protein maturation.

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Growth-based Determination and Biochemical Confirmation of Genetic Requirements for Protein Degradation in Saccharomyces cerevisiae
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Growth-based Determination and Biochemical Confirmation of Genetic Requirements for Protein Degradation in Saccharomyces cerevisiae

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Growth-based Determination and Biochemical Confirmation of Genetic Requirements for Protein Degradation in Saccharomyces cerevisiae
10:57

Growth-based Determination and Biochemical Confirmation of Genetic Requirements for Protein Degradation in Saccharomyces cerevisiae

Published on: February 16, 2015

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Cellular viability depends on precise protein folding, modification, and assembly during synthesis.
  • Sophisticated quality control mechanisms monitor protein maturation, degrading aberrant proteins to prevent toxicity.
  • Endoplasmic reticulum-associated degradation (ERAD) pathways are key to understanding protein quality control.

Purpose of the Study:

  • To elucidate the detailed mechanisms of protein recognition and degradation within ERAD pathways.
  • To establish a biochemical basis for understanding how misfolded proteins are identified and processed.
  • To clarify the cellular premise for distinguishing functional from non-functional proteins.

Main Methods:

  • Investigated substrate processing sites within ERAD pathways.
  • Analyzed glycan trimming steps as temporal regulators of protein folding.
  • Identified specific degradation signals on unfolded proteins.

Main Results:

  • Distinct substrate processing sites were discovered, providing a biochemical foundation for genetic profiles of misfolded proteins.
  • Sequential glycan trimming acts as a timer, allowing a window for proper protein folding.
  • Proteins failing to fold within the designated time expose a degradation signal recognized by ERAD.

Conclusions:

  • ERAD machinery recognizes proteins as aberrant based on delayed maturation, not direct detection of misfolding.
  • The system identifies proteins that have deviated from their normal folding pathways.
  • This mechanism ensures the removal of potentially toxic, improperly processed proteins, maintaining cellular health.