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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.

The TSC1-TSC2 complex consists of multiple TSC1 and TSC2 subunits