생화학분자생물학회입니다.
Diffusion-based determination of protein-protein interactions on reconstituted membrane surfaces
작성자
Jean K. Chung작성일자
2021-03-22조회수
194Name: Jean K. Chung ( jkchung@colostate.edu ) | ||
2019-present | Assistant Professor, Department of Chemistry, Colorado State University | |
2013-2018 | Postdoctoral Scholar, University of California Berkeley | |
2006-2012 | Ph.D., Chemistry, Stanford University |
Diffusion-based determination of protein-protein interactions on reconstituted membrane surfaces
The transient interactions between cellular components, particularly on membrane surfaces, are critical in the proper function of many biochemical reactions. For example, many signaling pathways involve dimerization, oligomerization, or other types of clustering of signaling proteins as a key step in the signaling cascade. However, it is often experimentally challenging to directly observe and characterize the molecular mechanisms such interactions—the greatest difficulty lies in the fact that living cells have an unknown number of background processes that may or may not participate in the molecular process of interest, and as a consequence, it is usually impossible to definitively correlate an observation to a well-defined cellular mechanism. One of the biophysical methods that can quantitatively capture these interactions is through membrane reconstitution, whereby a lipid bilayer is fabricated to mimic the membrane environment, and the biological components of interest are systematically introduced, without unknown background processes. This configuration allows the extensive use of fluorescence techniques, particularly fluorescence fluctuation spectroscopy and single-molecule fluorescence microscopy. In this review, we describe how the equilibrium diffusion of two proteins, K-Ras4B and the PH domain of Bruton’s tyrosine kinase (Btk), on fluid lipid membranes can be used to determine the kinetics of dimerization reactions.
https://pubmed.ncbi.nlm.nih.gov/33408000/
BMB Rep. 2021 Jan 7;5206. Online ahead of print.