uu.seUppsala University Publications
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Smad regulation in TGF-beta signal transduction
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Medicinska och farmaceutiska vetenskapsområdet, centrumbildningar mm, Ludwig Institute for Cancer Research.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Medicinska och farmaceutiska vetenskapsområdet, centrumbildningar mm, Ludwig Institute for Cancer Research.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Medicinska och farmaceutiska vetenskapsområdet, centrumbildningar mm, Ludwig Institute for Cancer Research.
2001 (English)In: Journal of Cell Science, ISSN 0021-9533, E-ISSN 1477-9137, Vol. 114, no Pt 24, 4359-4369 p.Article, review/survey (Other academic) Published
Abstract [en]

Smad proteins transduce signals from transforming growth factor-beta (TGF-beta) superfamily ligands that regulate cell proliferation, differentiation and death through activation of receptor serine/threonine kinases. Phosphorylation of receptor-activated Smads (R-Smads) leads to formation of complexes with the common mediator Smad (Co-Smad), which are imported to the nucleus. Nuclear Smad oligomers bind to DNA and associate with transcription factors to regulate expression of target genes. Alternatively, nuclear R-Smads associate with ubiquitin ligases and promote degradation of transcriptional repressors, thus facilitating target gene regulation by TGF-beta. Smads themselves can also become ubiquitinated and are degraded by proteasomes. Finally, the inhibitory Smads (I-Smads) block phosphorylation of R-Smads by the receptors and promote ubiquitination and degradation of receptor complexes, thus inhibiting signalling.

Place, publisher, year, edition, pages
2001. Vol. 114, no Pt 24, 4359-4369 p.
Keyword [en]
Activin Receptors; Type I/*metabolism/physiology, Animals, DNA-Binding Proteins/physiology, Humans, Phosphoproteins/physiology, Receptor Protein-Tyrosine Kinases/*metabolism/physiology, Receptors; Transforming Growth Factor beta/*metabolism/physiology, Research Support; Non-U.S. Gov't, Signal Transduction/*physiology, Trans-Activators/physiology, Transforming Growth Factor beta/*physiology
National Category
Medical and Health Sciences
Identifiers
URN: urn:nbn:se:uu:diva-73330PubMedID: 11792802OAI: oai:DiVA.org:uu-73330DiVA: diva2:101240
Available from: 2005-06-02 Created: 2005-06-02 Last updated: 2017-12-14Bibliographically approved

Open Access in DiVA

No full text

Other links

PubMedhttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Retrieve&list_uids=11792802&dopt=Citation

Authority records BETA

Moustakas, AristidisSouchelnytskyi, SerhiyHeldin, Carl-Henrik

Search in DiVA

By author/editor
Moustakas, AristidisSouchelnytskyi, SerhiyHeldin, Carl-Henrik
By organisation
Ludwig Institute for Cancer Research
In the same journal
Journal of Cell Science
Medical and Health Sciences

Search outside of DiVA

GoogleGoogle Scholar

pubmed
urn-nbn

Altmetric score

pubmed
urn-nbn
Total: 781 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf