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

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...

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Autores principales: Hoogeveen-Westerveld, Marianne, van Unen, Leontine, van den Ouweland, Ans, Halley, Dicky, Hoogeveen, Andre, Nellist, Mark
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3517901/
https://www.ncbi.nlm.nih.gov/pubmed/23006675
http://dx.doi.org/10.1186/1471-2091-13-18
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author Hoogeveen-Westerveld, Marianne
van Unen, Leontine
van den Ouweland, Ans
Halley, Dicky
Hoogeveen, Andre
Nellist, Mark
author_facet Hoogeveen-Westerveld, Marianne
van Unen, Leontine
van den Ouweland, Ans
Halley, Dicky
Hoogeveen, Andre
Nellist, Mark
author_sort Hoogeveen-Westerveld, Marianne
collection PubMed
description 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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spelling pubmed-35179012012-12-10 The TSC1-TSC2 complex consists of multiple TSC1 and TSC2 subunits Hoogeveen-Westerveld, Marianne van Unen, Leontine van den Ouweland, Ans Halley, Dicky Hoogeveen, Andre Nellist, Mark BMC Biochem Research Article 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. BioMed Central 2012-09-24 /pmc/articles/PMC3517901/ /pubmed/23006675 http://dx.doi.org/10.1186/1471-2091-13-18 Text en Copyright ©2012 Hoogeveen-Westerveld et al.; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Hoogeveen-Westerveld, Marianne
van Unen, Leontine
van den Ouweland, Ans
Halley, Dicky
Hoogeveen, Andre
Nellist, Mark
The TSC1-TSC2 complex consists of multiple TSC1 and TSC2 subunits
title The TSC1-TSC2 complex consists of multiple TSC1 and TSC2 subunits
title_full The TSC1-TSC2 complex consists of multiple TSC1 and TSC2 subunits
title_fullStr The TSC1-TSC2 complex consists of multiple TSC1 and TSC2 subunits
title_full_unstemmed The TSC1-TSC2 complex consists of multiple TSC1 and TSC2 subunits
title_short The TSC1-TSC2 complex consists of multiple TSC1 and TSC2 subunits
title_sort tsc1-tsc2 complex consists of multiple tsc1 and tsc2 subunits
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3517901/
https://www.ncbi.nlm.nih.gov/pubmed/23006675
http://dx.doi.org/10.1186/1471-2091-13-18
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