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
Interaction between Smad7 and beta-catenin: importance for transforming growth factor beta-induced apoptosis
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.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Medicinska och farmaceutiska vetenskapsområdet, centrumbildningar mm, Ludwig Institute for Cancer Research.
Show others and affiliations
2005 (English)In: Molecular and Cellular Biology, ISSN 0270-7306, E-ISSN 1098-5549, Vol. 25, no 4, 1475-1488 p.Article in journal (Refereed) Published
Abstract [en]

Members of the transforming growth factor beta (TGF-beta) and Wnt/wingless superfamilies regulate cell fate during development and tissue maintenance. Here we report that Smad7 interacts with beta-catenin and lymphoid enhancer binding factor 1/T-cell-specific factor (LEF1/TCF), transcriptional regulators in Wnt signaling, in a TGF-beta-dependent manner. Smad7 was found to be required for TGF-beta1-induced accumulation of beta-catenin and LEF1 in human prostate cancer (PC-3U) cells as well as in human keratinocytes (HaCaT cells). Moreover, when the endogenous Smad7 was repressed by specific small interfering RNA, TGF-beta-induced increase of activated p38, Akt phosphorylated on Ser473, glycogen synthase kinase 3beta phosphorylated on Ser9 was prevented, as well as the TGF-beta-induced association between beta-catenin and LEF1. Notably, the observed physical association of Smad7 and beta-catenin was found to be important for TGF-beta-induced apoptosis, since suppression of beta-catenin expression by small interfering RNA decreased the apoptotic response to TGF-beta.

Place, publisher, year, edition, pages
2005. Vol. 25, no 4, 1475-1488 p.
Keyword [en]
Animals, Apoptosis/drug effects/*physiology, COS Cells, Cell Fractionation, Cercopithecus aethiops, Cytoskeletal Proteins/*metabolism, DNA-Binding Proteins/*metabolism, Glycogen Synthase Kinase 3/metabolism, Humans, Male, Mice, Phosphorylation/drug effects, Prostatic Neoplasms/metabolism, Protein Binding/drug effects, Protein-Serine-Threonine Kinases/metabolism, Proto-Oncogene Proteins/metabolism, RNA; Small Interfering/metabolism, Research Support; Non-U.S. Gov't, Serine/metabolism, Trans-Activators/*metabolism, Transcription Factors/*metabolism, Transforming Growth Factor beta/*pharmacology, Tumor Cells; Cultured, p38 Mitogen-Activated Protein Kinases/metabolism
National Category
Medical and Health Sciences
Identifiers
URN: urn:nbn:se:uu:diva-72728DOI: 10.1128/MCB.25.4.1475-1488.2005PubMedID: 15684397OAI: oai:DiVA.org:uu-72728DiVA: diva2:100639
Available from: 2005-05-27 Created: 2005-05-27 Last updated: 2017-12-14Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full textPubMedhttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Retrieve&list_uids=15684397&dopt=Citation

Authority records BETA

Grimsby, SusanneAspenström, PontusHeldin, Carl-HenrikLandström, Maréne

Search in DiVA

By author/editor
Grimsby, SusanneAspenström, PontusHeldin, Carl-HenrikLandström, Maréne
By organisation
Ludwig Institute for Cancer Research
In the same journal
Molecular and Cellular Biology
Medical and Health Sciences

Search outside of DiVA

GoogleGoogle Scholar

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 605 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