Related Experiment Video
Updated: Jul 23, 2026

An In Vitro Dormancy Model of Estrogen-sensitive Breast Cancer in the Bone Marrow: A Tool for Molecular Mechanism Studies and Hypothesis Generation
Published on: June 30, 2015
Phosphorylation of basic fibroblast growth factor (FGF-2) in the nuclei of SK-Hep-1 cells
I Vilgrain1, A M Gonzalez, A Baird
1Department of Molecular and Cellular Growth Biology, Whittier Institute for Diabetes and Endocrinology, La Jolla, CA 92037.
Abstract:
The subcellular fractions containing protein kinases capable of phosphorylating basic fibroblast growth factor (FGF-2) are unknown, but having previously characterized one that is associated with the plasma membrane [1991, Mol. Endocrinol. 5, 1003-1012] we evaluated the catalytic properties of another in the nucleus. The reaction is time (linear up to 15 min), enzyme (2,000-25,000 nuclei/ml), and substrate (Km 0.18 microM) dependent, and the targets serine. DNase pretreatment of nuclei decreases the incorporation of phosphate into FGF-2 by 50% and the reaction. It is also inhibited by heparin (EC50 1 microgram/ml) and spermidine (EC50 3 microM). Calcium and cAMP have no effect. We conclude that the kinase is distinct from PKA, and PKC, and suggest that changes in glycosaminoglycan and polyamine concentrations during the cell cycle may modulate FGF-2 phosphorylation in the nucleus, or as it is translocated to the nucleus.
More Related Videos
07:32Screening and Identification of Small Peptides Targeting Fibroblast Growth Factor Receptor2 using a Phage Display Peptide Library
Published on: September 30, 2019
08:03Live-Cell Förster Resonance Energy Transfer Imaging of Metabolically Regulated Akt Activation Dynamics in HepG2 Cells
Published on: May 23, 2025
Related Concept Videos
Mitogens and the Cell Cycle
Regulation of Angiogenesis and Blood Supply
Introduction to Fibroblasts
Amplifying Signals via Second Messengers
TGF - β Signaling Pathway
Intracellular Signaling Affects Focal Adhesions
Some...