CHIP mediates degradation of Smad proteins and potentially regulates Smad-induced transcription (Q24603619)

2

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Xialian Xu

3

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Mei Huang

4

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Xinjun Zhang

5

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Yue Chen

6

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Shuping Zhang

7

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Xin-Yuan Fu

8

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Zhijie Chang

Molecular and Cellular Biology

9

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language of work or name

English

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publication date

January 2004

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published in

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volume

24

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issue

2

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page(s)

856-64

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cites work

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

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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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A novel smad nuclear interacting protein, SNIP1, suppresses p300-dependent TGF-beta signal transduction

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The Ski oncoprotein interacts with the Smad proteins to repress TGFbeta signaling

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Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions

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Dual role of the Smad4/DPC4 tumor suppressor in TGFbeta-inducible transcriptional complexes

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E2F4/5 and p107 as Smad cofactors linking the TGFbeta receptor to c-myc repression

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Direct interaction of c-Myc with Smad2 and Smad3 to inhibit TGF-beta-mediated induction of the CDK inhibitor p15(Ink4B)

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Smad regulation in TGF-beta signal transduction

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CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation

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c-Ski acts as a transcriptional co-repressor in transforming growth factor-beta signaling through interaction with smads

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A Smad transcriptional corepressor

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Smads: transcriptional activators of TGF-beta responses

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The oncoprotein Evi-1 represses TGF-beta signalling by inhibiting Smad3

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The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation

7 April 2017

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Transcriptional control by the TGF-beta/Smad signaling system

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Regulation of Smad activity

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SIP1, a novel zinc finger/homeodomain repressor, interacts with Smad proteins and binds to 5'-CACCT sequences in candidate target genes

27 September 2017

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TGF-beta-induced phosphorylation of Smad3 regulates its interaction with coactivator p300/CREB-binding protein

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CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein

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