Peptide Binding to Class I MHC Molecules
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Questions and Answers

Which proteins are targeted for proteolytic digestion by the ubiquitin-proteasome pathway?

  • Viral proteins only
  • Phagocytosed microbes only
  • Misfolded cytosolic and nuclear proteins only
  • All of the above (correct)

    • What happens to unfolded proteins in the cell?

  • They are degraded into peptides by the proteasomes (correct)
  • They are transported into the endoplasmic reticulum
  • They are targeted for proteolytic digestion by the ubiquitin-proteasome pathway
  • They are covalently tagged with ubiquitin

    • Which cells become very efficient at cleaving cytosolic and nuclear proteins into peptides?

  • All cells
  • Infected cells
  • Tumor cells
  • Cells exposed to inflammatory cytokines (correct)

    • Which molecule is responsible for transporting proteasome-generated peptides into the ER?

    <p>TAP molecules</p> Signup and view all the answers

    What is the function of tapasin in the peptide loading process?

    <p>It links MHC molecules to TAP molecules</p> Signup and view all the answers

    Why are empty class I MHC molecules eventually degraded in the ER?

    <p>They are unstable without bound peptides</p> Signup and view all the answers

    What happens when a class I MHC molecule binds tightly to a peptide generated from proteasomal digestion?

    <p>The peptide-MHC complex becomes stable and is delivered to the cell surface</p> Signup and view all the answers

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