scholarly journals Fibroblast growth factor receptor 3 regulates microtubule formation and cell surface mechanical properties in the developing organ of Corti

2012 ◽  
Vol 2 (6) ◽  
pp. 214-219 ◽  
Author(s):  
Katherine B. Szarama ◽  
Ruben Stepanyan ◽  
Ronald S. Petralia ◽  
Nuria Gavara ◽  
Gregory I. Frolenkov ◽  
...  
Keyword(s):  
Mechanical Properties ◽  
Growth Factor ◽  
Cell Surface ◽  
Fibroblast Growth Factor ◽  
Fibroblast Growth Factor Receptor ◽  
Growth Factor Receptor ◽  
Organ Of Corti ◽  
Fibroblast Growth ◽  
Microtubule Formation

Coexpression of Truncated Human Cytomegalovirus gH with the UL115 Gene Product or the Truncated Human Fibroblast Growth Factor Receptor Results in Transport of gH to the Cell Surface

Virology ◽  
1993 ◽  
Vol 193 (2) ◽  
pp. 853-861 ◽  
Author(s):  
Richard R. Spaete ◽  
Karen Perot ◽  
Patricia I. Scott ◽  
Jay A. Nelson ◽  
Mark F. Stinski ◽  
...  
Keyword(s):  
Growth Factor ◽  
Cell Surface ◽  
Fibroblast Growth Factor ◽  
Gene Product ◽  
Human Cytomegalovirus ◽  
Human Fibroblast ◽  
Fibroblast Growth Factor Receptor ◽  
Growth Factor Receptor ◽  
Fibroblast Growth

Retention in the Golgi apparatus and expression on the cell surface of Cfr/Esl-1/Glg-1/MG-160 are regulated by two distinct mechanisms

2011 ◽  
Vol 440 (1) ◽  
pp. 33-41 ◽  
Author(s):  
Yuichiro Miyaoka ◽  
Hidenori Kato ◽  
Kazuki Ebato ◽  
Shigeru Saito ◽  
Naoko Miyata ◽  
...  
Keyword(s):  
Growth Factor ◽  
Golgi Apparatus ◽  
Cell Surface ◽  
Fibroblast Growth Factor ◽  
Fibroblast Growth Factor Receptor ◽  
Growth Factor Receptor ◽  
Fibroblast Growth ◽  
Fgf Receptor ◽  
Juxtamembrane Region ◽  
Fgf Signalling

Cfr (cysteine-rich fibroblast growth factor receptor) is an Fgf (fibroblast growth factor)-binding protein without a tyrosine kinase. We have shown previously that Cfr is involved in Fgf18 signalling via Fgf receptor 3c. However, as Cfr is also known as Glg (Golgi apparatus protein)-1 or MG-160 and occurs in the Golgi apparatus, it remains unknown how the distribution of Cfr is regulated. In the present study, we performed a mutagenic analysis of Cfr to show that two distinct regions contribute to its distribution and stability. First, the C-terminal region retains Cfr in the Golgi apparatus. Secondly, the Cfr repeats in the extracellular juxtamembrane region destabilizes Cfr passed through the Golgi apparatus. This destabilization does not depend on the cleavage and secretion of the extracellular domain of Cfr. Furthermore, we found that Cfr with a GPI (glycosylphosphatidylinositol) anchor was predominantly expressed on the cell surface in Ba/F3 cells and affected Fgf18 signalling in a similar manner to the full-length Cfr, indicating that the interaction of Cfr with Fgfs on the cell surface is important for its function in Fgf signalling. These results suggest that the expression of Cfr in the Golgi apparatus and on the plasma membrane is finely tuned through two distinct mechanisms for exhibiting different functions.

scholarly journals Importin β–Mediated Nuclear Import of Fibroblast Growth Factor Receptor

2001 ◽  
Vol 152 (6) ◽  
pp. 1307-1312 ◽  
Author(s):  
John F. Reilly ◽  
Pamela A. Maher
Keyword(s):  
Signal Transduction ◽  
Growth Factor ◽  
Cell Surface ◽  
Fibroblast Growth Factor ◽  
Nuclear Import ◽  
Fibroblast Growth Factor Receptor ◽  
Nuclear Translocation ◽  
Growth Factor Receptor ◽  
Growth Factor Receptors ◽  
Fibroblast Growth

Although growth factor receptors are generally thought to carry out their role in signal transduction at the cell surface, many of these transmembrane proteins translocate to the nucleus after ligand stimulation. Here, we show that the nuclear translocation of fibroblast growth factor receptor (FGFR)1 occurs via a mechanism distinct from classical nuclear import but dependent on importin β, a component of multiple nuclear import pathways. Furthermore, we show that nuclear FGFR1 induces c-Jun and is involved in the regulation of cell proliferation. These data are the first description of a nuclear import pathway for transmembrane growth factor receptors and elucidate a novel signal transduction pathway from the cell surface to the nucleus.

Leupeptin enhances cell surface localization of fibroblast growth factor receptor 1 in adult sensory neurons by increased recycling

2012 ◽  
Vol 91 (2) ◽  
pp. 129-138 ◽  
Author(s):  
Barbara Hausott ◽  
Natalie Vallant ◽  
Margit Hochfilzer ◽  
Stefan Mangger ◽  
Regina Irschick ◽  
...  
Keyword(s):  
Growth Factor ◽  
Cell Surface ◽  
Fibroblast Growth Factor ◽  
Sensory Neurons ◽  
Fibroblast Growth Factor Receptor ◽  
Growth Factor Receptor ◽  
Fibroblast Growth ◽  
Surface Localization ◽  
Cell Surface Localization

scholarly journals Thyroid hormone increases fibroblast growth factor receptor expression and disrupts cell mechanics in the developing organ of corti

2013 ◽  
Vol 13 (1) ◽  
pp. 6 ◽  
Author(s):  
Katherine B Szarama ◽  
Núria Gavara ◽  
Ronald S Petralia ◽  
Richard S Chadwick ◽  
Matthew W Kelley
Keyword(s):  
Growth Factor ◽  
Thyroid Hormone ◽  
Fibroblast Growth Factor ◽  
Cell Mechanics ◽  
Fibroblast Growth Factor Receptor ◽  
Growth Factor Receptor ◽  
Organ Of Corti ◽  
Receptor Expression ◽  
Fibroblast Growth
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