Kinetics of the early events of GPCR signalling

被引:12
作者
Adamson, Roslin J. [1 ]
Watts, Anthony [1 ]
机构
[1] Univ Oxford, Dept Biochem, Biomembrane Struct Unit, Oxford OX1 3QU, England
基金
英国惠康基金;
关键词
G protein-coupled receptor; Electron microscopy; Surface plasmon resonance; Nanodisc; G protein; PROTEIN-COUPLED RECEPTORS; DELTA-OPIOID RECEPTOR; MEMBRANE-PROTEINS; PLASMON RESONANCE; LIGAND-BINDING; NEUROTENSIN; NANODISCS; RECONSTITUTION; PURIFICATION; RHODOPSIN;
D O I
10.1016/j.febslet.2014.10.043
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Neurotensin receptor type 1 (NTS1) is a G protein-coupled receptor (GPCR) that affects cellular responses by initiating a cascade of interactions through G proteins. The kinetic details for these interactions are not well-known. Here, NTS1-nanodisc-G alpha(s) and G alpha(i1) interactions were studied. The binding affinities of G alpha(i1) and G alpha(s) to NTS1 were directly measured by surface plasmon resonance (SPR) and determined to be 15 +/- 6 nM and 31 +/- 18 nM, respectively. This SPR configuration permits the kinetics of early events in signalling pathways to be explored and can be used to initiate descriptions of the GPCR interactome. (C) 2014 The Authors. Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
引用
收藏
页码:4701 / 4707
页数:7
相关论文
共 61 条
[1]   Plasmon resonance methods in GPCR signaling and other membrane events [J].
Alves, ID ;
Park, CK ;
Hruby, VJ .
CURRENT PROTEIN & PEPTIDE SCIENCE, 2005, 6 (04) :293-312
[2]   Selectivity, cooperativity, and reciprocity in the interactions between the δ-opioid receptor, its ligands, and G-proteins [J].
Alves, ID ;
Ciano, KA ;
Boguslavski, V ;
Varga, E ;
Salamon, Z ;
Yamamura, HI ;
Hruby, VJ ;
Tollin, G .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (43) :44673-44682
[3]   Different structural states of the proteolipid membrane are produced by ligand binding to the human δ-opioid receptor as shown by plasmon-waveguide resonance spectroscopy [J].
Alves, ID ;
Cowell, SM ;
Salamon, Z ;
Devanathan, S ;
Tollin, G ;
Hruby, VJ .
MOLECULAR PHARMACOLOGY, 2004, 65 (05) :1248-1257
[4]   Direct observation of G-protein binding to the human δ-opioid receptor using plasmon-waveguide resonance spectroscopy [J].
Alves, ID ;
Salamon, Z ;
Varga, E ;
Yamamura, HI ;
Tollin, G ;
Hruby, VJ .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (49) :48890-48897
[5]   Improved yield of a ligand-binding GPCR expressed in E. coli for structural studies [J].
Attrill, Helen ;
Harding, Peter J. ;
Smith, Eleanor ;
Ross, Simon ;
Watts, Anthony .
PROTEIN EXPRESSION AND PURIFICATION, 2009, 64 (01) :32-38
[6]   Rapid incorporation of functional rhodopsin into nanoscale apolipoprotein bound bilayer (NABB) particles [J].
Banerjee, Sourabh ;
Huber, Thomas ;
Sakmar, Thomas P. .
JOURNAL OF MOLECULAR BIOLOGY, 2008, 377 (04) :1067-1081
[7]   Self-assembly of discoidal phospholipid bilayer nanoparticles with membrane scaffold proteins [J].
Bayburt, TH ;
Grinkova, YV ;
Sligar, SG .
NANO LETTERS, 2002, 2 (08) :853-856
[8]   Membrane protein assembly into Nanodiscs [J].
Bayburt, Timothy H. ;
Sligar, Stephen G. .
FEBS LETTERS, 2010, 584 (09) :1721-1727
[9]   Nanodiscs for immobilization of lipid bilayers and membrane receptors: Kinetic analysis of cholera toxin binding to a glycolipid receptor [J].
Borch, Jonas ;
Torta, Federico ;
Sligar, Stephen G. ;
Roepstorff, Peter .
ANALYTICAL CHEMISTRY, 2008, 80 (16) :6245-6252
[10]   The nanodisc: a novel tool for membrane protein studies [J].
Borch, Jonas ;
Hamann, Thomas .
BIOLOGICAL CHEMISTRY, 2009, 390 (08) :805-814