Related Experiment Video
Updated: Jan 21, 2026

Co-Translational Insertion of Membrane Proteins into Preformed Nanodiscs
Published on: November 19, 2020
Peptide-based NTA(Ni)-nanodiscs for studying membrane enhanced FGFR1 kinase activities
Juanjuan Liu1,2, Lei Zhu1, Xueli Zhang3,4
1High Magnetic Field Laboratory, Key Laboratory of High Magnetic Field and Ion Beam Physical Biology, Hefei Institutes of Physical Science, Chinese Academy of Sciences, Hefei, Anhui, China.
Abstract:
Tyrosine autophosphorylation plays a crucial regulatory role in the kinase activities of fibroblast growth factor receptors (FGFRs), and in the recruitment and activation of downstream intracellular signaling pathways. Biophysical and biochemical investigations of FGFR kinase domains in membrane environments offer key insights into phosphorylation mechanisms. Hence, we constructed nickel chelating nanodiscs based on a 22-residue peptide. The spontaneous anchoring of N-terminal His6-tagged FGFR1c kinase domain (FGFR1K) onto peptide nanodiscs grants FGFR1K orientations occurring on native plasma membranes. Following membrane incorporation, the autophosphorylation of FGFR1K, as exemplified by Y653 and Y654 in the A-loop and the total tyrosine phosphorylation, increase significantly. This in vitro reconstitution system may be applicable to studies of other membrane associated phenomena.
Related Concept Videos
Protein Kinases and Phosphatases
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein Kinases and Phosphatases
Peptide Bonds
Acid–Base Equilibria: Activity-Based Definition of pH
In solutions of very low ionic strength—for example, pure water—the...
Receptor Tyrosine Kinases
Self-Evaluation: Self-Enhancement and Self-Verification

