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TMEM106B aggregation in neurodegenerative diseases: linking genetics to function.

Hai-Shan Jiao1, Peng Yuan2, Jin-Tai Yu3

  • 1Department of Neurology and National Center for Neurological Disorders, Huashan Hospital, State Key Laboratory of Medical Neurobiology and MOE Frontiers Center for Brain Science, Shanghai Medical College, Fudan University, Shanghai, 200040, China.

Molecular Neurodegeneration
|August 10, 2023
PubMed
Summary
This summary is machine-generated.

Mutations in the TMEM106B gene are linked to neurodegenerative diseases. New research suggests TMEM106B protein aggregation, not loss-of-function, disrupts cellular processes and offers a potential therapeutic target.

Keywords:
AggregationAmyloid fibrilsLysosomeNeurodegenerationTMEM106BTherapeutics

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Area of Science:

  • Neuroscience
  • Genetics
  • Cell Biology

Background:

  • Mutations in TMEM106B are established risk factors for neurodegenerative diseases.
  • Prior research focused on TMEM106B loss-of-function impairing lysosome biogenesis.
  • The mechanism linking increased TMEM106B expression from mutations to functional disruption remained unclear.

Purpose of the Study:

  • To systematically review existing literature on TMEM106B function in health and disease.
  • To explore the role of TMEM106B protein aggregation in neurodegeneration.
  • To propose a novel mechanism for TMEM106B-related pathology.

Main Methods:

  • Systematic review of scientific literature.
  • Analysis of studies reporting TMEM106B protein aggregation.
  • Integration of findings on TMEM106B mutations and lysosomal function.

Main Results:

  • TMEM106B proteins form intracellular amyloid filaments in various neurodegenerative diseases.
  • These amyloid filaments can be the predominant form of protein aggregation.
  • TMEM106B aggregations may recruit and interfere with normal TMEM106B protein function.

Conclusions:

  • TMEM106B mutations contribute to lysosome dysfunction primarily through promoting TMEM106B aggregation.
  • Reducing TMEM106B aggregation presents a potential therapeutic strategy.
  • Targeting TMEM106B aggregation could restore lysosomal function and treat neurodegenerative diseases.