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Diffusion-based determination of protein homodimerization on reconstituted membrane surfaces

정진경|Tyler A. Jepson
생화학분자생물학회 (Korean Society Of Biochemistry And Molecular Biology)|2021.03|BMB Reports|제54권 제3호|pp. 157-163

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키워드

Fluorescence correlation spectroscopyDimerizationIn vitro membrane reconstitutionSingle molecule tracking
주제분류화학

초록

The transient interactions between cellular components, particularlyon membrane surfaces, are critical in the proper functionof many biochemical reactions. For example, many signalingpathways involve dimerization, oligomerization, or othertypes of clustering of signaling proteins as a key step in the signalingcascade. However, it is often experimentally challengingto directly observe and characterize the molecular mechanismssuch interactions—the greatest difficulty lies in the fact that livingcells have an unknown number of background processes thatmay or may not participate in the molecular process of interest,and as a consequence, it is usually impossible to definitivelycorrelate an observation to a well-defined cellular mechanism. One of the experimental methods that can quantitatively capturethese interactions is through membrane reconstitution, wherebya lipid bilayer is fabricated to mimic the membrane environment,and the biological components of interest are systematically introduced,without unknown background processes. This configurationallows the extensive use of fluorescence techniques, particularlyfluorescence fluctuation spectroscopy and single-moleculefluorescence microscopy. In this review, we describe how theequilibrium diffusion of two proteins, K-Ras4B and the PH domainof Bruton’s tyrosine kinase (Btk), on fluid lipid membranescan be used to determine the kinetics of homodimerizationreactions.

Abstract

The transient interactions between cellular components, particularlyon membrane surfaces, are critical in the proper functionof many biochemical reactions. For example, many signalingpathways involve dimerization, oligomerization, or othertypes of clustering of signaling proteins as a key step in the signalingcascade. However, it is often experimentally challengingto directly observe and characterize the molecular mechanismssuch interactions—the greatest difficulty lies in the fact that livingcells have an unknown number of background processes thatmay or may not participate in the molecular process of interest,and as a consequence, it is usually impossible to definitivelycorrelate an observation to a well-defined cellular mechanism. One of the experimental methods that can quantitatively capturethese interactions is through membrane reconstitution, wherebya lipid bilayer is fabricated to mimic the membrane environment,and the biological components of interest are systematically introduced,without unknown background processes. This configurationallows the extensive use of fluorescence techniques, particularlyfluorescence fluctuation spectroscopy and single-moleculefluorescence microscopy. In this review, we describe how theequilibrium diffusion of two proteins, K-Ras4B and the PH domainof Bruton’s tyrosine kinase (Btk), on fluid lipid membranescan be used to determine the kinetics of homodimerizationreactions.

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