Assistance for Folding of Disease-Causing Plasma Membrane Proteins

Karina Juarez-Navarro1, Victor M Ayala-Garcia1, Estela Ruiz-Baca1

  • 1Facultad de Ciencias Quimicas, Universidad Juarez del Estado de Durango, Durango C.P 34000, Mexico.

Biomolecules
|May 13, 2020
PubMed

Insights

Plasma membrane (PM) protein mutations cause disease through misfolding and aggregation. This review covers PM protein processing, its failures, and therapeutic strategies using chaperones and drugs to restore proteostasis.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Pathology

Background:

  • Mutations in plasma membrane (PM) proteins are linked to various diseases.
  • These mutations often lead to incorrect protein folding and localization, causing cellular dysfunction.
  • Protein aggregation resulting from these defects can be toxic to cells.

Purpose of the Study:

  • To review the processing of PM proteins from synthesis to delivery.
  • To highlight the consequences of PM protein processing failures in disease.
  • To summarize current therapeutic strategies for correcting misassembled PM proteins.

Main Methods:

  • Review of scientific literature on PM protein processing and related diseases.
  • Analysis of the impact of protein folding and localization defects.
  • Summary of therapeutic approaches involving chaperones and small molecule drugs.

Main Results:

  • PM protein processing involves synthesis, folding, and transport.
  • Failures in this pathway lead to protein misassembly, aggregation, and cellular dysfunction.
  • Therapeutic strategies aim to enhance protein quality control and proteostasis.

Conclusions:

  • Understanding PM protein processing is crucial for disease etiology.
  • Targeting protein folding and quality control offers therapeutic potential.
  • Chaperones and small molecules are key in developing strategies to rescue misfolded proteins.

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