scholarly journals Identification of Ribosome-binding Protein p34 as an Intracellular Protein That Binds Acidic Fibroblast Growth Factor

2002 ◽  
Vol 277 (26) ◽  
pp. 23864-23871 ◽  
Author(s):  
Camilla Skiple Skjerpen ◽  
Jørgen Wesche ◽  
Sjur Olsnes
1998 ◽  
Vol 336 (1) ◽  
pp. 213-222 ◽  
Author(s):  
Elona KOLPAKOVA ◽  
Antoni WIĘDŁOCHA ◽  
Harald STENMARK ◽  
Olav KLINGENBERG ◽  
Pål Ø. FALNES ◽  
...  

In addition to its extracellular action, there is evidence that acidic fibroblast growth factor (aFGF) acts inside cells. To identify intracellular proteins interacting with aFGF, we screened a HeLa cell library in the yeast two-hybrid system using pLex-aFGF as a bait. A clone binding to aFGF, but not to the non-mitogenic mutant aFGF-K132E, was isolated and characterized. The insert contained an open reading frame corresponding to a novel protein of 42 kDa. The protein, termed aFGF intracellular binding protein (FIBP), is mainly hydrophilic and does not contain an N-terminal signal sequence. In vitro-translated FIBP bound specifically to a fusion protein of maltose-binding protein and aFGF. FIBP became post-translationally associated with microsomes added to the cell-free protein synthesizing system, and the membrane-associated protein bound aFGF with high efficiency. Immunoblots and fluorescence microscopy demonstrated that the protein is present in nuclei and, to a lesser extent, associated with mitochondria and other cytoplasmic membranes. The possibility is discussed that FIBP may be involved in the mitogenic action of aFGF. The nucleotide sequences described in this paper have been submitted to GeneBank database under accession numbers AF010187 (human FIBP) and AF010188 (simian FIBP).


2000 ◽  
Vol 352 (3) ◽  
pp. 629-635 ◽  
Author(s):  
Elona KOLPAKOVA ◽  
Eirik FRENGEN ◽  
Trond STOKKE ◽  
Sjur OLSNES

Acidic fibroblast growth factor (aFGF) intracellular binding protein (FIBP) is a protein found mainly in the nucleus that might be involved in the intracellular function of aFGF. Here we present a comparative analysis of the deduced amino acid sequences of human, murine and Drosophila FIBP analogues and demonstrate that FIBP is an evolutionarily conserved protein. The human gene spans more than 5kb, comprising ten exons and nine introns, and maps to chromosome 11q13.1. Two slightly different splice variants found in different tissues were isolated and characterized. Sequence analysis of the region surrounding the translation start revealed a CpG island, a classical feature of widely expressed genes. Functional studies of the promoter region with a luciferase reporter system suggested a strong transcriptional activity residing within 600bp of the 5´ flanking region.


2000 ◽  
Vol 275 (50) ◽  
pp. 39801
Author(s):  
Violaine K. Harris ◽  
Christine M. Coticchia ◽  
Heinz-Joachim List ◽  
Anton Wellstein ◽  
Anna Tate Riegel

Sign in / Sign up

Export Citation Format

Share Document