(Q24299213)

SMAD protein signal transduction

GOA release 2020-03-11

1 reference

GOA release 2020-03-11

author name string

Hong Bing Chen

1

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Jonathan G Rud

2

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Kai Lin

3

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Lan Xu

Journal of Biological Chemistry

4

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language of work or name

English

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publication date

3 June 2005

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published in

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volume

280

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issue

22

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page(s)

21329-36

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cites work

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Signal transduction by the TGF-beta superfamily

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MADR2 is a substrate of the TGFbeta receptor and its phosphorylation is required for nuclear accumulation and signaling

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

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Partnership between DPC4 and SMAD proteins in TGF-beta signalling pathways.

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Crystal Structure of a Phosphorylated Smad2

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The L3 loop and C-terminal phosphorylation jointly define Smad protein trimerization

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Structural basis of heteromeric smad protein assembly in TGF-beta signaling

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Smads: transcriptional activators of TGF-beta responses

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TGF-beta signaling from a three-dimensional perspective: insight into selection of partners

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Distinct oligomeric states of SMAD proteins in the transforming growth factor-beta pathway

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Smad2 nucleocytoplasmic shuttling by nucleoporins CAN/Nup214 and Nup153 feeds TGFbeta signaling complexes in the cytoplasm and nucleus

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Nucleocytoplasmic shuttling of Smads 2, 3, and 4 permits sensing of TGF-beta receptor activity

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Analysis of Smad nucleocytoplasmic shuttling in living cells

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The nuclear import function of Smad2 is masked by SARA and unmasked by TGFbeta-dependent phosphorylation.

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Regulating access to the genome: nucleocytoplasmic transport throughout the cell cycle

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Transport between the cell nucleus and the cytoplasm

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Nucleocytoplasmic transport: the soluble phase

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Peering through the Pore

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Distinct domain utilization by Smad3 and Smad4 for nucleoporin interaction and nuclear import.

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Transforming growth factor-beta induces nuclear import of Smad3 in an importin-beta1 and Ran-dependent manner

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An extended bipartite nuclear localization signal in Smad4 is required for its nuclear import and transcriptional activity

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Importin beta mediates nuclear translocation of Smad 3

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A distinct nuclear localization signal in the N terminus of Smad 3 determines its ligand-induced nuclear translocation

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Transforming growth factor beta-independent shuttling of Smad4 between the cytoplasm and nucleus.

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Regulation of intracellular dynamics of Smad4 by its leucine-rich nuclear export signal

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Smad3 allostery links TGF-beta receptor kinase activation to transcriptional control

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The asymmetric distribution of the constituents of the Ran system is essential for transport into and out of the nucleus

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Dominant-negative mutants of importin-beta block multiple pathways of import and export through the nuclear pore complex

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Inhibition of in vitro nuclear transport by a lectin that binds to nuclear pores

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Human Smad3 and Smad4 are sequence-specific transcription activators

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CRM1 is an export receptor for leucine-rich nuclear export signals

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Nucleocytoplasmic shuttling factors including Ran and CRM1 mediate nuclear export of NFAT In vitro

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DPC4, a candidate tumor suppressor gene at human chromosome 18q21.1

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Missense mutations of MADH4: characterization of the mutational hot spot and functional consequences in human tumors

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Smad4/DPC4 silencing and hyperactive Ras jointly disrupt transforming growth factor-beta antiproliferative responses in colon cancer cells.

21 January 2018

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Crystal structure of a Smad MH1 domain bound to DNA: insights on DNA binding in TGF-beta signaling

21 January 2018

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Ubiquitin-dependent degradation of TGF-beta-activated smad2.

21 January 2018

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NF-AT activation requires suppression of Crm1-dependent export by calcineurin

21 January 2018

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Crystal structure of a phosphorylated Smad2. Recognition of phosphoserine by the MH2 domain and insights on Smad function in TGF-beta signaling

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