Abstract
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.
Original language | Undefined/Unknown |
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Journal | BMC Biochemistry |
Volume | 13 |
DOIs | |
Publication status | Published - 2012 |
Research programs
- EMC MGC-02-96-01