Regulation of Smad degradation and activity by Smurf2, an E3 ubiquitin ligase
about
A novel link between the proteasome pathway and the signal transduction pathway of the bone morphogenetic proteins (BMPs).Ablation of Smurf2 reveals an inhibition in TGF-β signalling through multiple mono-ubiquitination of Smad3CHIP controls the sensitivity of transforming growth factor-beta signaling by modulating the basal level of Smad3 through ubiquitin-mediated degradationThe forkhead transcription factor FOXO4 induces the down-regulation of hypoxia-inducible factor 1 alpha by a von Hippel-Lindau protein-independent mechanismUSP15 stabilizes TGF-β receptor I and promotes oncogenesis through the activation of TGF-β signaling in glioblastomaAn RNF11: Smurf2 complex mediates ubiquitination of the AMSH proteinPin1 down-regulates transforming growth factor-beta (TGF-beta) signaling by inducing degradation of Smad proteinsIdentification of novel Smad2 and Smad3 associated proteins in response to TGF-beta1Protein associated with SMAD1 (PAWS1/FAM83G) is a substrate for type I bone morphogenetic protein receptors and modulates bone morphogenetic protein signallingJab1 antagonizes TGF-beta signaling by inducing Smad4 degradationSmurf2 up-regulation activates telomere-dependent senescenceThe novel E3 ubiquitin ligase Tiul1 associates with TGIF to target Smad2 for degradationSmad3 recruits the anaphase-promoting complex for ubiquitination and degradation of SnoNCHIP mediates degradation of Smad proteins and potentially regulates Smad-induced transcriptionArkadia amplifies TGF-beta superfamily signalling through degradation of Smad7Insulin-induced phosphorylation of FKHR (Foxo1) targets to proteasomal degradationInduction by transforming growth factor-beta1 of epithelial to mesenchymal transition is a rare event in vitroMolecular pathogenesis of hepatocellular carcinoma and impact of therapeutic advancesKey role for ubiquitin protein modification in TGFβ signal transductionRegulation of TGF-β Superfamily Signaling by SMAD Mono-UbiquitinationOveractive bone morphogenetic protein signaling in heterotopic ossification and Duchenne muscular dystrophyTargeting TGF-β signaling in cancerMicroRNA-208 modulates BMP-2-stimulated mouse preosteoblast differentiation by directly targeting V-ets erythroblastosis virus E26 oncogene homolog 1Activation of transforming growth factor-beta signaling by SUMO-1 modification of tumor suppressor Smad4/DPC4Lung Krüppel-like factor contains an autoinhibitory domain that regulates its transcriptional activation by binding WWP1, an E3 ubiquitin ligaseTGF-beta induces assembly of a Smad2-Smurf2 ubiquitin ligase complex that targets SnoN for degradationAn expanded WW domain recognition motif revealed by the interaction between Smad7 and the E3 ubiquitin ligase Smurf2Transcriptional induction of Smurf2 ubiquitin ligase by TGF-betaNegative regulation of transforming growth factor-beta (TGF-beta) signaling by WW domain-containing protein 1 (WWP1)Smurf2 induces ubiquitin-dependent degradation of Smurf1 to prevent migration of breast cancer cellsRepulsive guidance molecule (RGMa), a DRAGON homologue, is a bone morphogenetic protein co-receptorUbiquitin ligase Smurf1 controls osteoblast activity and bone homeostasis by targeting MEKK2 for degradationOncogenic herpesvirus KSHV Hijacks BMP-Smad1-Id signaling to promote tumorigenesisThe FYVE domain of Smad Anchor for Receptor Activation (SARA) is required to prevent skin carcinogenesis, but not in mouse developmentTGF-Beta Negatively Regulates the BMP2-Dependent Early Commitment of Periodontal Ligament Cells into Hard Tissue Forming CellsComprehensive functional characterization of cancer-testis antigens defines obligate participation in multiple hallmarks of cancerThe TGF-β Signaling Regulator PMEPA1 Suppresses Prostate Cancer Metastases to BoneEngulfment protein GULP is regulator of transforming growth factor-β response in ovarian cells.HECT E3s and human disease.USP15 regulates SMURF2 kinetics through C-lobe mediated deubiquitination.
P2860
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P2860
Regulation of Smad degradation and activity by Smurf2, an E3 ubiquitin ligase
description
2001 nî lūn-bûn
@nan
2001 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Regulation of Smad degradation and activity by Smurf2, an E3 ubiquitin ligase
@ast
Regulation of Smad degradation and activity by Smurf2, an E3 ubiquitin ligase
@en
Regulation of Smad degradation and activity by Smurf2, an E3 ubiquitin ligase
@en-gb
Regulation of Smad degradation and activity by Smurf2, an E3 ubiquitin ligase
@nl
type
label
Regulation of Smad degradation and activity by Smurf2, an E3 ubiquitin ligase
@ast
Regulation of Smad degradation and activity by Smurf2, an E3 ubiquitin ligase
@en
Regulation of Smad degradation and activity by Smurf2, an E3 ubiquitin ligase
@en-gb
Regulation of Smad degradation and activity by Smurf2, an E3 ubiquitin ligase
@nl
prefLabel
Regulation of Smad degradation and activity by Smurf2, an E3 ubiquitin ligase
@ast
Regulation of Smad degradation and activity by Smurf2, an E3 ubiquitin ligase
@en
Regulation of Smad degradation and activity by Smurf2, an E3 ubiquitin ligase
@en-gb
Regulation of Smad degradation and activity by Smurf2, an E3 ubiquitin ligase
@nl
P2093
P2860
P3181
P356
P1476
Regulation of Smad degradation and activity by Smurf2, an E3 ubiquitin ligase
@en
P2093
A Hemmati-Brivanlou
D J Gehling
P2860
P3181
P356
10.1073/PNAS.98.3.974
P407
P577
2001-01-30T00:00:00Z