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- 저자 : Finkielstein, Carla V. (검색결과 3 건)
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Azurmendi, Hugo F.,Mitra, Sharmistha,Ayala, Iriscilla,Li, Liwu,Finkielstein, Carla V.,Capelluto, Daniel G.S. Korean Society for Molecular and Cellular Biology 2010 Molecules and cells Vol.30 No.6
The Toll-interacting protein (Tollip) is a negative regulator of the Toll-like receptor (TLR)-mediated inflammation response. Tollip is a modular protein that contains an N-terminal $\underline{T}om1$-$\underline{b}inding$ $\underline{d}omain$ (TBD), a central $\underline{c}$onserved domain $\underline{2}$ (C2), and a C-terminal $\underline{c}$oupling of $\underline{u}$biquitin to $\underline{e}$ndoplasmic reticulum degradation (CUE) domain. Here, we report the sequence-specific backbone $^1H$, $^{15}N$, and $^{13}C$ assignments of the human Tollip CUE domain. The CUE domain was found to be a stable dimer as determined by size-exclusion chromatography and molecular cross-linking studies. Analysis of the backbone chemical shift data indicated that the CUE domain exhibits three helical elements corresponding to 52% of the protein backbone. Circular dichroism spectrum analysis confirmed the helical nature of this domain. Comparison of the location of these helical regions with those reported for yeast CUE domains suggest differences in length for all helical elements. We expect the structural analysis presented here will be the foundation for future studies on the biological significance of the Tollip CUE domain, its molecular interactions, and the mechanisms that modulate its function during the inflammatory response.
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Hugo F. Azurmendi,Sharmistha Mitra,Iriscilla Ayala,Liwu Li,Carla V. Finkielstein,Daniel G.S. Capelluto 한국분자세포생물학회 2010 Molecules and cells Vol.30 No.6
The Toll-interacting protein (Tollip) is a negative regulator of the Toll-like receptor (TLR)-mediated inflammation response. Tollip is a modular protein that contains an Nterminal Tom1-binding domain (TBD), a central conserved domain 2 (C2), and a C-terminal coupling of ubiquitin to endoplasmic reticulum degradation (CUE) domain. Here,we report the sequence-specific backbone 1H, 15N, and 13C assignments of the human Tollip CUE domain. The CUE domain was found to be a stable dimer as determined by size-exclusion chromatography and molecular crosslinking studies. Analysis of the backbone chemical shift data indicated that the CUE domain exhibits three helical elements corresponding to 52% of the protein backbone. Circular dichroism spectrum analysis confirmed the helical nature of this domain. Comparison of the location of these helical regions with those reported for yeast CUE domains suggest differences in length for all helical elements. We expect the structural analysis presented here will be the foundation for future studies on the biological significance of the Tollip CUE domain, its molecular interactions,and the mechanisms that modulate its function during the inflammatory response.
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Gotoh, Tetsuya,Kim, Jae Kyoung,Liu, Jingjing,Vila-Caballer, Marian,Stauffer, Philip E.,Tyson, John J.,Finkielstein, Carla V. National Academy of Sciences 2016 PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF Vol.113 No.47
<P>The circadian clock and cell cycle networks are interlocked on the molecular level, with the core clock loop exerting a multilevel regulatory role over cell cycle components. This is particularly relevant to the circadian factor Period 2 (Per2), which modulates the stability of the tumor suppressor p53 in unstressed cells and transcriptional activity in response to genotoxic stress. Per2 binding prevents Mdm2-mediated ubiquitination of p53 and, therefore, its degradation, and oscillations in the peaks of Per2 and p53 were expected to correspond. However, our findings showed that Per2 and p53 rhythms were significantly out-of-phase relative to each other in cell lysates and in purified cytoplasmic fractions. These seemingly conflicting experimental data motivated the use of a combined theoretical and experimental approach focusing on the role played by Per2 in dictating the phase of p53 oscillations. Systematic modeling of all possible regulatory scenarios predicted that the observed phase relationship between Per2 and p53 could be simulated if (i) p53 was more stable in the nucleus than in the cytoplasm, (ii) Per2 associates to various ubiquitinated forms of p53, and (iii) Per2 mediated p53 nuclear import. These predictions were supported by a sevenfold increase in p53's half-life in the nucleus and by in vitro binding of Per2 to the various ubiquitinated forms of p53. Last, p53's nuclear shuttling was significantly favored by ectopic expression of Per2 and reduced because of Per2 down-regulation. Our combined theoretical/mathematical approach reveals how clock regulatory nodes can be inferred from oscillating time course data.</P>
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