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
Translocated in liposarcoma (TLS) is a substrate for fibroblast growth factor receptor-1.
Uppsala University, Medicinska vetenskapsområdet, Faculty of Medicine, Department of Genetics and Pathology. Uppsala University, Medicinska vetenskapsområdet, Faculty of Medicine, Department of Genetics and Pathology. (Vascular Biology)
Ludwiginstitutet för Cancerforskning.
Ludwiginstitutet för Cancerforskning.
Show others and affiliations
2004 (English)In: Cell Signal, ISSN 0898-6568, Vol. 16, no 4, 515-20 p.Article in journal (Other scientific) Published
Abstract [en]

Binding of fibroblast growth factor (FGF) to the high affinity receptor-1 (FGFR-1) leads to activation of its endogenous tyrosine kinase activity. A number of substrates for the FGFR-1 kinase have been identified. Among those, FGF receptor-substrate-2 (FRS-2) was identified by virtue of its interaction with p13suc, a yeast protein involved in cell cycle regulation. We have used immobilized p13suc to identify a new substrate for FGRF-1, which is identical to "translocated in liposarcoma" (TLS). TLS is a RNA/DNA-binding protein which occurs in fusion products with different transcription factors in a variety of solid tumours. We show that TLS is tyrosine phosphorylated in intact cells by a number of different growth factors, indicating a role in growth regulation.

Place, publisher, year, edition, pages
2004. Vol. 16, no 4, 515-20 p.
Keyword [en]
Animals, Cell Fractionation, Fibroblast Growth Factors/*metabolism, Liposarcoma/*metabolism, Membrane Proteins/*metabolism, Mice, Phosphoproteins/*metabolism, Phosphorylation, Receptor Protein-Tyrosine Kinases/*metabolism, Receptors; Fibroblast Growth Factor/*metabolism, Research Support; Non-U.S. Gov't, Research Support; U.S. Gov't; P.H.S., Swiss 3T3 Cells, Tyrosine/metabolism
Identifiers
URN: urn:nbn:se:uu:diva-72992PubMedID: 14709340OAI: oai:DiVA.org:uu-72992DiVA: diva2:100903
Available from: 2005-05-31 Created: 2005-05-31 Last updated: 2011-01-12

Open Access in DiVA

No full text

Other links

PubMedhttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Retrieve&list_uids=14709340&dopt=Citation

Authority records BETA

Hellman, UlfWernstedt, ChristerClaesson-Welsh, Lena

Search in DiVA

By author/editor
Hellman, UlfWernstedt, ChristerClaesson-Welsh, Lena
By organisation
Department of Genetics and Pathology

Search outside of DiVA

GoogleGoogle Scholar

pubmed
urn-nbn

Altmetric score

pubmed
urn-nbn
Total: 753 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