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Updated: Mar 24, 2026

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The VPS35 protein and the role of its impairments in mitochondrial dysfunction in Parkinson's disease

O A Buneeva1, A E Medvedev1

  • 1Institute of Biomedical Chemistry, Moscow, Russia.

Biomeditsinskaia Khimiia
|March 17, 2026
PubMed

Insights

VPS35 protein is crucial for cellular functions and mitochondrial health. Mutations in VPS35 are linked to Parkinson's disease, affecting neuronal survival and retromer function.

Area of Science:

  • Cell Biology
  • Neuroscience
  • Biochemistry

Background:

  • VPS35 is a vital protein, central to the retromer complex, facilitating protein recycling.
  • VPS35 also regulates mitochondrial homeostasis and dynamics, impacting cellular function.
  • Mutations in VPS35, like D620N, are implicated in Parkinson's disease pathogenesis.

Purpose of the Study:

  • To review the structure and function of the retromer complex.
  • To elucidate the role of VPS35 in mitochondrial regulation.
  • To analyze VPS35 interactions with Parkinson's disease-associated proteins.

Main Methods:

  • Literature review of existing studies on VPS35, retromer complex, and Parkinson's disease.
  • Analysis of structural and functional data related to VPS35.
  • Examination of protein-protein interactions involving VPS35 and mitochondrial proteins.

Main Results:

  • VPS35 is essential for endosome-to-TGN and endosome-to-plasma membrane protein trafficking.
  • VPS35 plays a significant role in maintaining mitochondrial integrity and dynamics.
  • VPS35 dysfunction, particularly via mutations, contributes to neurodegeneration observed in Parkinson's disease.

Conclusions:

  • VPS35 is a key player in both protein trafficking and mitochondrial health.
  • Understanding VPS35's interactions is critical for deciphering Parkinson's disease mechanisms.
  • Targeting VPS35 pathways may offer therapeutic strategies for Parkinson's disease.
Keywords:
VPS35mitochondriamitochondrial dysfunctionneurodegenerationretromer complex

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