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Updated: May 18, 2026

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
Published on: November 28, 2017
The TSC1-TSC2 complex consists of multiple TSC1 and TSC2 subunits
Marianne Hoogeveen-Westerveld1, Leontine van Unen, Ans van den Ouweland
1Department of Clinical Genetics, Erasmus Medical Centre, Dr, Molewaterplein 50, Rotterdam, 3015 GE, The Netherlands.
Background:
Mutations to the TSC1 and TSC2 genes cause the disease tuberous sclerosis complex. The TSC1 and TSC2 gene products form a protein complex that integrates multiple metabolic signals to regulate the activity of the target of rapamycin (TOR) complex 1 (TORC1) and thereby control cell growth. Here we investigate the quaternary structure of the TSC1-TSC2 complex by gel filtration and coimmunoprecipitation.
Results:
TSC1 and TSC2 co-eluted in high molecular weight fractions by gel filtration. Coimmunoprecipitation of distinct tagged TSC1 and TSC2 isoforms demonstrated that TSC1-TSC2 complexes contain multiple TSC1 and TSC2 subunits.
Conclusions:
TSC1 and TSC2 interact to form large complexes containing multiple TSC1 and TSC2 subunits.
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