Premium
Cysteine‐rich FGF receptor regulates intracellular FGF‐1 and FGF‐2 levels
Author(s) -
Zuber Michael E.,
Zhou Zhaohui,
Burrus Laura W.,
Olwin Bradley B.
Publication year - 1997
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/(sici)1097-4652(199703)170:3<217::aid-jcp1>3.0.co;2-r
Subject(s) - intracellular , microbiology and biotechnology , fibroblast growth factor , biology , receptor , chinese hamster ovary cell , cell surface receptor , mutant , biochemistry , gene
The cysteine‐rich FGF receptor (CFR) is a 150‐kD membrane‐associated glycoprotein that specifically binds FGFs. CFR protein is not detectable at the cell surface and immunocytochemistry with anti‐CFR antibodies demonstrates that CFR is concentrated in the Golgi apparatus. These data suggest CFR does not function as a plasma membrane FGF receptor. CFR expressed in chinese hamster ovary cells reduces the intracellular accumulation of exogenously applied FGF‐1 and FGF‐2. A mutant CFR lacking the juxtamembrane, transmembrane and intracellular domains is unable to alter intracellular FGF levels. Mutant CFR is detected throughout the cell, indicating that the domains absent in mutant CFR are required for appropriate subcellular localization and the regulation of intracellular FGF levels. Although the activation of plasma membrane receptors is necessary for cellular responses to FGFs, a requirement for intracellular FGF has also been proposed. The subcellular localization of CFR and its ability to regulate the levels of intracellular FGFs suggests that CFR may be involved in intracellular FGF trafficking and the regulation of cellular responses to FGFs. J. Cell. Physiol. 170:217–227, 1997. © 1997 Wiley‐Liss, Inc.