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Single octapeptide deletion selectively processes a pathogenic prion protein mutant on the cell surface

Yumi Lee1, Duri Lee1, Ilho Choi1

  • 1Department of Biomedical Sciences, University of Ulsan College of Medicine & Asan Institute of Life Sciences, Asan Medical Center, Seoul, Republic of Korea.

Biochemical and Biophysical Research Communications
|January 18, 2016
PubMed

Insights

A single octapeptide repeat deletion in prion protein (PrP) does not alter PrP levels alone. However, this mutation affects the cell surface processing and distribution of specific PrP mutants.

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Genetics

Background:

  • Prion diseases are linked to aberrant prion protein (PrP) metabolism.
  • The role of octapeptide repeats in PrP metabolism is not fully understood.

Purpose of the Study:

  • To investigate the impact of octapeptide repeat mutations on PrP metabolism.
  • To explore how these mutations affect PrP processing and cellular localization.

Main Methods:

  • Deletion mutation of a single octapeptide repeat in the PRNP gene in HeLa cells.
  • Analysis of PrP levels, synthesis, distribution, and processing.

Main Results:

  • A single octapeptide repeat deletion mutation alone did not affect overall PrP levels.
  • This deletion selectively reduced PrP levels in the presence of other pathogenic mutations.
  • The A117V PrP mutant showed altered cell surface distribution and processing with the octapeptide deletion.

Conclusions:

  • Octapeptide repeat number influences PrP metabolism in a mutation-dependent manner.
  • The study reveals novel insights into mutant-specific PrP metabolism on the cell surface.
Keywords:
Octapeptide repeatsPrionProteostasisSecretory pathway

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