The TSC1-TSC2 complex: a molecular switchboard controlling cell growth.

By Jingxiang Huang, B. Manning. Biochemical Journal, 2008

1,242 citations recorded by the source corpus.

Subfields: Immunology, Molecular Biology, Physiology

View Paper: https://www.semanticscholar.org/paper/5995ad2f5eb5b4e95a5a50d07a6d852b718fb653

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Immunology

1. J. Asara
2. D. Morrison
3. I. Ben-Sahra
4. Jessica J. Howell
5. B. Manning
6. Lewis C. Cantley
7. David M. Sabatini
8. Alec C. Kimmelman

In Molecular Biology

1. David M. Sabatini
2. R. A. Saxton
3. B. Manning
4. Lewis C. Cantley
5. Jingxiang Huang
6. D. Morrison
7. Ping Wee
8. Zhixiang Wang

In Physiology

1. David M. Sabatini
2. B. Manning
3. R. A. Saxton
4. J. Asara
5. D. Morrison
6. I. Ben-Sahra
7. Jessica J. Howell
8. Lewis C. Cantley

Citations in the corpus

• Epidermal Growth Factor Receptor Cell Proliferation Signaling Pathways (2017, background): “TSC1 and TSC2 suppress the activity of RHEB (Ras-like GTPase), which are needed to activate mTORC1 [287].”
• Stimulation of de novo pyrimidine synthesis by growth signaling through mTOR and S6K1 (2013, methodology): “To reveal additional inputs from the mTORC1 pathway into the control of cellular metabolism, we used unbiased metabolomic profiling in cells lacking the tuberous sclerosis complex 2 (TSC2) tumor suppressor, a key negative regulator of mTORC1 (5).”
• Phosphatidylinositol-5-phosphate 4-kinases regulate cellular lipid metabolism by facilitating autophagy (2018, background): “TSC2 is a negative regulator of mTORC1 activity and siRNA knockdown of TSC2 increases downstream activation of mTORC1 targets (Huang and Manning, 2008, 2009).”
• The 14-3-3 proteins: integrators of diverse signaling cues that impact cell fate and cancer development (2008, background): “Also functioning upstream of TORC1 is the tuberous sclerosis complex TSC1–TSC2, which inhibits TORC1 signaling as a result of the GTPase-activating protein (GAP) activity that is intrinsic to TSC2 and that inactivates Rheb [19].”
• A complex interplay between Akt, TSC2, and the two mTOR complexes (2009, background): “majority of published experiments, phosphorylation of these sites does not affect the association between TSC1 and TSC2 (reviewed in [16].”
• mTOR Signaling in Growth, Metabolism, and Disease. (2017, background): “2A, reviewed in Huang and Manning, 2008), including the insulin/insulin-like growth factor-1 (IGF-1) pathway, which triggers the Akt-dependent multisite phosphorylation of TSC2.”
• Bidirectional Transport of Amino Acids Regulates mTOR and Autophagy (2009, positive): “Two key growth factor signals that regulate the mTORC1 pathway emanate from the insulin/insulin-like growth factor (IGF) 1/phosphatidyl inositol-3-OH kinase (PI(3)K) and extracellular signal regulated kinase-p90 ribosomal protein S6 kinase (ERK-RSK) pathways (Huang and Manning, 2008).”