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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2021.1
- 수록면
- 157 - 163 (7page)
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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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참고문헌 (69)
참고문헌 신청
Eyster KM / 2007 / The membrane and lipids as integral participants in signal transduction : lipid signal transduction for the non-lipid biochemist / Adv Physiol Educ 31:5~16
Groves JT / 2010 / Molecular mechanisms in signal transduction at the membrane / Nat Struct Mol Biol 17:659~665
Cho W / 2005 / Membrane-protein interactions in cell signaling and membrane trafficking / Annu Rev Biophys Biomol Struct 34:119~151
Kasai RS / 2018 / The Class-A GPCR Dopamine D2 Receptor Forms Transient Dimers Stabilized by Agonists : Detection by Single-Molecule Tracking / Cell Biochem Biophys 76:29~37
Freed DM / 2017 / EGFR Ligands Differentially Stabilize Receptor Dimers to Specify Signaling Kinetics / Cell 171:683.e618~695.e618
Groves JT / 2010 / Molecular mechanisms in signal transduction at the membrane / Nat Struct Mol Biol 17:659~665
Cho W / 2005 / Membrane-protein interactions in cell signaling and membrane trafficking / Annu Rev Biophys Biomol Struct 34:119~151
Kasai RS / 2018 / The Class-A GPCR Dopamine D2 Receptor Forms Transient Dimers Stabilized by Agonists : Detection by Single-Molecule Tracking / Cell Biochem Biophys 76:29~37
Freed DM / 2017 / EGFR Ligands Differentially Stabilize Receptor Dimers to Specify Signaling Kinetics / Cell 171:683.e618~695.e618
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