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Related Experiment Videos

SUMO-1 modification increases human SOD1 stability and aggregation.

Erkang Fei1, Nali Jia, Ming Yan

  • 1Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230027, People's Republic of China.

Biochemical and Biophysical Research Communications
|July 11, 2006
PubMed
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SUMO-1 modification of copper-zinc superoxide dismutase (SOD1) increases its stability and aggregation. This sumoylation process may contribute to the motor neuron loss seen in familial amyotrophic lateral sclerosis (FALS).

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Genetics

Background:

  • Mutations in copper-zinc superoxide dismutase (SOD1) cause familial amyotrophic lateral sclerosis (FALS).
  • Mutant SOD1 forms inclusions in FALS patient tissues, but the accumulation mechanism is unclear.

Purpose of the Study:

  • To investigate the role of SUMO-1 modification in SOD1 stability and aggregation.
  • To determine if SUMO-1 modification contributes to FALS pathogenesis.

Main Methods:

  • Investigated SOD1 as a SUMO-1 substrate.
  • Mutated lysine 75 in SOD1 to abolish sumoylation.
  • Assessed the effect of SUMO-1 modification on SOD1 levels and aggregation.

Main Results:

  • Human SOD1 is modified by SUMO-1.

Related Experiment Videos

  • Mutation of lysine 75 prevents SOD1 sumoylation.
  • SUMO-1 modification increases both wild-type and mutant SOD1 levels and aggregation.
  • SUMO-1 co-localizes with SOD1 aggregates.

    • Conclusions:

    • SUMO-1 modification of SOD1, particularly at lysine 75, regulates its stability and aggregation.
    • Sumoylation of SOD1 may play a role in the pathogenesis of FALS associated with mutant SOD1.