Protein sensors for membrane sterols.

By J. Goldstein, R. DeBose-Boyd, Michael S. Brown. Cell, 2006

1,658 citations recorded by the source corpus.

Subfields: Molecular Biology, Surgery

View Paper: https://www.semanticscholar.org/paper/c0ef712e33703133c10ca786ab5f85950c69e9e0

How researchers see this paper

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

In Molecular Biology

1. R. Kaufman
2. J. Malhotra
3. P. Tontonoz
4. J. Goldstein
5. Navdeep S. Chandel
6. Michael S. Brown
7. Ralph J. Deberardinis
8. S. Bensinger

In Surgery

1. J. Malhotra
2. P. Tontonoz
3. J. Goldstein
4. Michael S. Brown
5. R. Kaufman
6. Chunming Cheng
7. Deliang Guo
8. Xiang Cheng

Citations in the corpus

• The endoplasmic reticulum and the unfolded protein response. (2007, background): “The proteases S1P and S2P were originally identified for their essential role in processing of the sterol response element binding protein (SREBP) transcription factor, which is activated upon cholesterol deprivation [44] (Fig.”
• Thyroid hormone regulation of metabolism. (2014, background): “Another regulator of the LDL-R gene is the sterol response element binding protein (SREBP)-2 (97).”
• Cellular cholesterol trafficking and compartmentalization (2008, background): “The ER cholesterol concentration appears to control several functions that are related to the ER and ER–Golgi membrane transport, such as the operation of the sterol-homeostatic machiner”
• LXR signaling couples sterol metabolism to proliferation in the acquired immune response (2008, background): “Brown and Goldstein have delineated an elegant mechanism for the regulation of cholesterol synthesis in which SREBP is held as an inactive precursor in the ER by the sterol-sensing protein SCAP (Goldstein et al., 2006).”
• Structure of N-terminal Domain of NPC1 Reveals Distinct Subdomains for Binding and Transfer of Cholesterol (2009, background): “The liberated cholesterol must then exit the lysosomal compartment in order to reach the plasma membrane and the endoplasmic reticulum (ER) where it performs structural and regulatory roles, respectively (Demel and De Kruyff, 1976; Simons and Ikonen, 2000; Goldstein et al., 2006).”
• Mechanistic insights into the generation and transduction of Hedgehog Signaling (2020, background): “Notably, TMs 2–6 of PTCH1 and DISP1 form sterol-sensing domains (SSDs) that share sequence homology with other membrane proteins in cholesterol metabolism and signaling, including Niemann-Pick disease, type C1 (NPC1) protein, Niemann-Pick disease, type C1-like 1 (NPC1L1) protein, HMG-CoA reductase, ”
• The Endoplasmic Reticulum: Folding, Calcium Homeostasis, Signaling, and Redox Control (2006, neutral): “…ASK1, apoptosis signal-regulating kinase 1; BAP, BiP-associated protein; Bax, Bcl-associated factor, Bcl, B-cell lymphoma; bHLH, basic helix–loop–helix; BiP/GRP78, immunoglobulin heavy chain binding protein/glucose regulated protein 78; cADPR, cyclic ADP-ribose; CCE, capacitative Ca 2+ entry;…”
• Endoplasmic Reticulum Stress and Oxidative Stress: A Vicious Cycle or a Double-Edged Sword? (2007, positive): “The proteases S1P and S2P were originally identified for their essential role in processing of the sterol response element binding protein (SREBP) transcription factor, that is activated on cholesterol deprivation (37) (see Fig.”
• Akt stimulates hepatic SREBP1c and lipogenesis through parallel mTORC1-dependent and independent pathways (2011, neutral): “SREBP1c regulation is quite complex (Goldstein et al., 2006; Raghow et al., 2008).”
• A Century of Cholesterol and Coronaries: From Plaques to Genes to Statins (2015, positive): “SREBP Pathway Elucidated Over the next few years, we solved the movement problem, and the result is the SREBP pathway shown in Figures 3A and 3B (Brown and Goldstein, 1997; Goldstein et al., 2006).”
• Network analysis of the MVA and MEP pathways for isoprenoid synthesis. (2013, background): “In the ER, SREBP forms complexes with SREBP cleavage-activating protein (Scap), another ER protein that ensures transport of SREBP to the Golgi apparatus when sterol levels are depleted.”
• The role for endoplasmic reticulum stress in diabetes mellitus. (2008, result): “LeeK,TirasophonW,ShenX,MichalakM,PrywesR,OkadaT, YoshidaH,MoriK, KaufmanRJ2002IRE1-mediatedunconven- tionalmRNAsplicingandS2P-mediatedATF6cleavagemergeto regulateXBP1insignalingtheunfoldedproteinresponse.”