| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
J. Biol. Chem., Vol. 277, Issue 26, 23864-23871, June 28, 2002
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
From the Department of Biochemistry, Institute for Cancer Research,
Norwegian Radium Hospital, Montebello, 0310 Oslo, Norway
With the aim of identifying new intracellular
binding partners for acidic fibroblast growth factor (aFGF), proteins
from U2OS human osteosarcoma cells were adsorbed to immobilized aFGF.
One of the adsorbed proteins is a member of the leucine-rich repeat protein family termed ribosome-binding protein p34 (p34). This protein
has previously been localized to endoplasmic reticulum membranes and is
thought to span the membrane with the N terminus on the cytosolic side.
Confocal microscopy of cells transfected with Myc-p34 confirmed the
endoplasmic reticulum localization, and Northern blotting determined
p34 mRNA to be present in a multitude of different tissues.
Cross-linking experiments indicated that the protein is present in the
cell as a dimer. In vitro translated p34 was found to
interact with maltose-binding protein-aFGF through its cytosolic
coiled-coil domain. The interaction between aFGF and p34 was further
characterized by surface plasmon resonance, giving a
KD of 1.4 ± 0.3 µM. Even though
p34 interacted with mitogenic aFGF, it bound poorly to the
non-mitogenic aFGF(K132E) mutant, indicating a possible involvement of
p34 in intracellular signaling by aFGF.
Identification of Ribosome-binding Protein p34 as an
Intracellular Protein That Binds Acidic Fibroblast Growth Factor*
,, and
*
This work was supported by the Norwegian Cancer Society, the
Novo Nordisk Foundation, the Norwegian Research Council for Science and
Humanities, Blix Legat, Rachel and Otto Kr. Bruun's Legat, and the
Jahre Foundation.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Fellow of the Norwegian Cancer Society.
§
To whom correspondence should be addressed. Tel.: 47-22-93-5640;
Fax: 47-22-50-8692; E-mail: sjur.olsnes@labmed.uio.no.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  T. Nilsen, K. R. Rosendal, V. Sorensen, J. Wesche, S. Olsnes, and A. Wiedlocha A Nuclear Export Sequence Located on a beta-Strand in Fibroblast Growth Factor-1 J. Biol. Chem., September 7, 2007; 282(36): 26245 - 26256. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 V. Sorensen, A. Wiedlocha, E. M. Haugsten, D. Khnykin, J. Wesche, and S. Olsnes Different abilities of the four FGFRs to mediate FGF-1 translocation are linked to differences in the receptor C-terminal tail J. Cell Sci., October 15, 2006; 119(20): 4332 - 4341. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. Joliot Transduction Peptides Within Naturally Occurring Proteins Sci. Signal., December 6, 2005; 2005(313): pe54 - pe54. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. Wiedlocha, T. Nilsen, J. Wesche, V. Sorensen, J. Malecki, E. Marcinkowska, and S. Olsnes Phosphorylation-regulated Nucleocytoplasmic Trafficking of Internalized Fibroblast Growth Factor-1 Mol. Biol. Cell, February 1, 2005; 16(2): 794 - 810. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 S. Olsnes, O. Klingenberg, and A. Wiedlocha Transport of Exogenous Growth Factors and Cytokines to the Cytosol and to the Nucleus Physiol Rev, January 1, 2003; 83(1): 163 - 182. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |
