Cited by 24Tuberous Sclerosis Complex ResearchPI3K/AKT/mTOR signaling in cancerHippo pathway signaling and YAP/TAZ

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

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Hoogeveen-Westerveld, Marianne, van Unen, Leontine, van den Ouweland, Ans, Halley, Dicky, Hoogeveen, Andre, Nellist, Mark·2012·BMC Biochemistry

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.

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Crossref · 10.1186/1471-2091-13-18

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  • Chromatographic analyses suggest that TSCCs also contain multiple copies of TSC1 and TSC2, and it is postulated that including multiple copies of each constituent protein may increase the sensitivity of the complex to allosteric regulation.

    “Chromatographic analyses suggest that TSCCs also contains multiple copies of TSC1 and TSC2, and it is postulated that including multiple copies of each constituent protein may increase the sensitivity of the complex to allosteric regulation (Hoogeveen-Westerveld et al., 2012).”

    From Signal integration in the (m)TORC1 growth pathway (2018) · cites this paper as Hoogeveen-Westerveld et al., 2012

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Authors
Hoogeveen-Westerveld, M., van Unen, L., van den Ouweland, A., Halley, D., Hoogeveen, A., & Nellist, M.
Affiliations
Erasmus MC (NL)
Corresponding author
Nellist, Mark
Venue
BMC Biochemistry
Published
2012-09-24
Volume
13
Issue
1
Pages
18-18
ISSN
1471-2091 (ISSN-L)
OpenAlex
W2132804463
Cited by
24
References
35
Citations by year
2025: 1 · 2023: 1 · 2022: 1 · 2021: 3 · 2019: 3 · 2018: 4 · 2016: 5 · 2015: 2 · 2014: 3 · 2013: 1
FWCI
1.29
Type
journal article
Language
en
Open access
Licence
cc-by
Locations
  • BMC Biochemistry (publishedVersion, cc-by)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • EUR Research Repository (Erasmus University Rotterdam) (submittedVersion, other-oa)
  • RePub (Erasmus University Rotterdam) (submittedVersion, other-oa)
Topics
  • Health Sciences › Medicine › Physiology › Tuberous Sclerosis Complex Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hippo pathway signaling and YAP/TAZ
Keywords
TSC1/TSC2 complex, tuberous sclerosis complex, cell growth regulation, protein-protein interaction, molecular weight
MeSH terms
Tuberous Sclerosis Complex 1 Protein, Tuberous Sclerosis Complex 2 Protein, Epitopes, Chromatography, Gel, Humans, Protein Isoforms, Protein Structure, Quaternary, Tumor Suppressor Proteins, Immunoprecipitation, HEK293 Cells, TOR Serine-Threonine Kinases

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