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Translocated in liposarcoma (TLS) is a substrate for fibroblast growth factor receptor-1.

Journal article
Authors Peter Klint
Ulf Hellman
Christer Wernstedt
Pierre Åman
David Ron
Lena Claesson-Welsh
Published in Cellular signalling
Volume 16
Issue 4
Pages 515-20
ISSN 0898-6568
Publication year 2004
Published at Institute of Laboratory Medicine, Dept of Pathology
Pages 515-20
Language en
Links dx.doi.org/10.1016/j.cellsig.2003.0...
Keywords Adaptor Proteins, Signal Transducing, Animals, Cell Fractionation, Fibroblast Growth Factors, metabolism, Liposarcoma, metabolism, Membrane Proteins, metabolism, Mice, Phosphoproteins, metabolism, Phosphorylation, Receptor Protein-Tyrosine Kinases, metabolism, Receptor, Fibroblast Growth Factor, Type 1, Receptors, Fibroblast Growth Factor, metabolism, Swiss 3T3 Cells, Tyrosine, metabolism
Subject categories Medical and Health Sciences

Abstract

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.

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