Analysis of TSC1 truncations defines regions involved in TSC1 stability, aggregation and interaction
Open accessAbstract
Tuberous sclerosis complex (TSC) is an autosomal dominant disorder characterised by the development of hamartomas in a variety of organs and tissues. The disease is caused by mutations in either the TSC1 gene on chromosome 9q34, or the TSC2 gene on chromosome 16p13.3. The TSC1 and TSC2 gene products, TSC1 and TSC2, interact to form a protein complex that inhibits signal transduction to the downstream effectors of the target of rapamycin complex 1 (TORC1). Here we investigate TSC1 structure and function by analysing a series of truncated TSC1 proteins. We identify specific regions of the protein that are important for TSC1 stability, localisation, interactions and function.
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The TSC1 core domain is considered essential for the stability of TSC1.
“The core domain is considered essential for the stability of TSC1 (Hoogeveen-Westerveld et al., 2010; Mozaffari et al., 2009);”
From Signal integration in the (m)TORC1 growth pathway (2018) · cites this paper as Hoogeveen-Westerveld et al., 2010
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References 25 · Cited by 25
- Authors
- Hoogeveen-Westerveld, M., Exalto, C., Maat-Kievit, A., van den Ouweland, A., Halley, D., & Nellist, M.
- Affiliations
- Erasmus MC (NL)
- Corresponding author
- Nellist, Mark
- Venue
- Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease
- Publisher
- Elsevier BV
- Published
- 2010-09
- Volume
- 1802
- Issue
- 9
- Pages
- 774-781
- ISSN
- 0925-4439 (ISSN-L)
- OpenAlex
- W2140113816
- Cited by
- 25
- References
- 25
- Citations by year
- 2024: 2 · 2023: 1 · 2021: 1 · 2020: 1 · 2019: 1 · 2018: 2 · 2017: 2 · 2016: 3 · 2015: 2 · 2014: 3 · 2013: 3 · 2012: 1
- FWCI
- 1.52
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease (publishedVersion)
- PubMed (publishedVersion)
- EUR Research Repository (Erasmus University Rotterdam) (submittedVersion)
- HAL (submittedVersion, other-oa)
- Trinity's Access to Research Output (TARA) (Trinity College Dublin) (submittedVersion)
- Funders
- U.S. Department of Defense Congressionally-Directed Medical Research Program (#TS060052)
- 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, tuberous sclerosis complex, protein truncation, protein stability, protein aggregation, protein-protein interaction, TORC1 inhibition, TSC2
- MeSH terms
- Tuberous Sclerosis Complex 1 Protein, Tuberous Sclerosis Complex 2 Protein, Cells, Cultured, Humans, Protein Binding, Structure-Activity Relationship, Gene Deletion, Protein Structure, Tertiary, Tumor Suppressor Proteins, Protein Interaction Mapping, Genomic Instability, Mutant Proteins, Protein Multimerization, Protein Stability
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