期刊
BIOPHYSICAL JOURNAL
卷 78, 期 4, 页码 1881-1894出版社
BIOPHYSICAL SOCIETY
DOI: 10.1016/S0006-3495(00)76737-3
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- NIDDK NIH HHS [DK 51067, DK 45881, DK37206] Funding Source: Medline
In search of the structural basis for gating of amiloride-sensitive Na+ channels, kinetic properties of single homo and heterooligomeric ENaCs formed by the subunits with individual truncated cytoplasmic domains were studied in a cell-free planar lipid bilayer reconstitution system. Our results identify the N-terminus of the alpha-subunit as a major determinant of kinetic behavior of both homooligomeric and heterooligomeric ENaCs, although the carboxy-terminal domains of beta- and gamma-ENaC subunits play important role(s) in modulation of the kinetics of heterooligomeric channels. We also found that the cystic fibrosis transmembrane conductance regulator (CFTR) inhibits amiloride-sensitive channels, at least in part, by modulating their gating. Comparison of these data suggests that the modulatory effects of the beta- and gamma-ENaC subunits, and of the CFTR, may involve the same, or closely related, mechanism(s); namely, locking the heterooligomeric channels in their closed state. These mechanisms, however, do not completely override the gating mechanism of the alpha-channel.
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