Smurf1 regulates the inhibitory activity of Smad7 by targeting Smad7 to the plasma membrane (Q24303055)

SMAD specific E3 ubiquitin protein ligase 1

GOA release 2020-03-11

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GOA release 2020-03-11

I-SMAD binding

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GOA release 2020-03-11

author name string

Chie Suzuki

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Gyo Murakami

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Minoru Fukuchi

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Tomomasa Shimanuki

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Yuko Shikauchi

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Takeshi Imamura

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Kohei Miyazono

Journal of Biological Chemistry

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language of work or name

English

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publication date

18 October 2002

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published in

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volume

277

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issue

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page(s)

39919-25

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cites work

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Betaglycan presents ligand to the TGF beta signaling receptor.

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TGF-beta signaling by Smad proteins

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Substrate targeting in the ubiquitin system

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Crystal structure of the PTEN tumor suppressor: implications for its phosphoinositide phosphatase activity and membrane association

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Smads: transcriptional activators of TGF-beta responses

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Smads as transcriptional co-modulators

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Nedd4-like proteins: an emerging family of ubiquitin-protein ligases implicated in diverse cellular functions

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Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGF beta receptor for degradation

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Genetic approaches to TGFbeta signaling pathways

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The DSmurf ubiquitin-protein ligase restricts BMP signaling spatially and temporally during Drosophila embryogenesis.

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A SMAD ubiquitin ligase targets the BMP pathway and affects embryonic pattern formation

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TGF-beta induces assembly of a Smad2-Smurf2 ubiquitin ligase complex that targets SnoN for degradation

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TGF-β signalling from cell membrane to nucleus through SMAD proteins

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Smad6 inhibits signalling by the TGF-β superfamily

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Identification of Smad7, a TGFbeta-inducible antagonist of TGF-beta signalling

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Deadly encounter: ubiquitin meets apoptosis

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Regulation of Smad degradation and activity by Smurf2, an E3 ubiquitin ligase

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The C2 domain of the ubiquitin protein ligase Nedd4 mediates Ca2+-dependent plasma membrane localization

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Regulation of Smad7 promoter by direct association with Smad3 and Smad4.

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Smad6 is a Smad1/5-induced smad inhibitor. Characterization of bone morphogenetic protein-responsive element in the mouse Smad6 promoter

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Smurf2 is a ubiquitin E3 ligase mediating proteasome-dependent degradation of Smad2 in transforming growth factor-beta signaling

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Smurf1 interacts with transforming growth factor-beta type I receptor through Smad7 and induces receptor degradation

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Multiple WW domains, but not the C2 domain, are required for inhibition of the epithelial Na+ channel by human Nedd4

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Identification of developmentally expressed proteins that functionally interact with Nedd4 ubiquitin ligase

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Membrane targeting by C1 and C2 domains

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The N domain of Smad7 is essential for specific inhibition of transforming growth factor-beta signaling

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Ligand-dependent degradation of Smad3 by a ubiquitin ligase complex of ROC1 and associated proteins

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Smad proteins exist as monomers in vivo and undergo homo- and hetero-oligomerization upon activation by serine/threonine kinase receptors

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7 January 2021

Smad6 inhibits BMP/Smad1 signaling by specifically competing with the Smad4 tumor suppressor

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Multiple, distinct forms of bovine and human protein kinase C suggest diversity in cellular signaling pathways

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https://api.crossref.org/works/10.1074%2FJBC.M201901200

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TGF-beta signal transduction

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Identifiers

DOI

10.1074/JBC.M201901200

1 reference

Consolidated OpenCitations Corpus – April 2017

release_juj3efopy5e7fglpdh2exw335a

Fatcat ID

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/juj3efopy5e7fglpdh2exw335a

24 November 2022

mapped directly with Wikidata item

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

12151385

1 reference

Consolidated OpenCitations Corpus – April 2017