Spatial distribution and activity of Na+/K+-ATPase in lipid bilayer membranes with phase boundaries
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Spatial distribution and activity of Na+/K+-ATPase in lipid bilayer membranes with phase boundaries. / Bhatia, Tripta; Cornelius, Flemming; Brewer, Jonathan; Bagatolli, Luis A.; Simonsen, Adam C.; Ipsen, John H.; Mouritsen, Ole G.
In: Biochimica et Biophysica Acta - Biomembranes, Vol. 1858, No. 6, 2016, p. 1390-1399.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Spatial distribution and activity of Na+/K+-ATPase in lipid bilayer membranes with phase boundaries
AU - Bhatia, Tripta
AU - Cornelius, Flemming
AU - Brewer, Jonathan
AU - Bagatolli, Luis A.
AU - Simonsen, Adam C.
AU - Ipsen, John H.
AU - Mouritsen, Ole G.
PY - 2016
Y1 - 2016
N2 - We have reconstituted functional Na +/K +-ATPase (NKA) into giant unilamellar vesicles (GUVs) of well-defined binary and ternary lipid composition including cholesterol. The activity of the membrane system can be turned on and off by ATP. The hydrolytic activity of NKA is found to depend on membrane phase, and the water relaxation in the membrane on the presence of NKA. By collapsing and fixating the GUVs onto a solid support and using high-resolution atomic-force microscopy (AFM) imaging we determine the protein orientation and spatial distribution at the single-molecule level and find that NKA is preferentially located at l o/l d interfaces in two-phase GUVs and homogeneously distributed in single-phase GUVs. When turned active, the membrane is found to unbind from the support suggesting that the protein function leads to softening of the membrane.
AB - We have reconstituted functional Na +/K +-ATPase (NKA) into giant unilamellar vesicles (GUVs) of well-defined binary and ternary lipid composition including cholesterol. The activity of the membrane system can be turned on and off by ATP. The hydrolytic activity of NKA is found to depend on membrane phase, and the water relaxation in the membrane on the presence of NKA. By collapsing and fixating the GUVs onto a solid support and using high-resolution atomic-force microscopy (AFM) imaging we determine the protein orientation and spatial distribution at the single-molecule level and find that NKA is preferentially located at l o/l d interfaces in two-phase GUVs and homogeneously distributed in single-phase GUVs. When turned active, the membrane is found to unbind from the support suggesting that the protein function leads to softening of the membrane.
KW - Domains
KW - Giant unilamellar vesicles
KW - Membrane biophysics
KW - Membrane protein
KW - Membranes
KW - Na /K -ATPase
KW - Protein-lipid interaction
U2 - 10.1016/j.bbamem.2016.03.015
DO - 10.1016/j.bbamem.2016.03.015
M3 - Journal article
C2 - 26994932
AN - SCOPUS:84962476173
VL - 1858
SP - 1390
EP - 1399
JO - B B A - Biomembranes
JF - B B A - Biomembranes
SN - 0005-2736
IS - 6
ER -
ID: 230974172