منابع مشابه
CFTR Gating II
Previously, we demonstrated that ADP inhibits cystic fibrosis transmembrane conductance regulator (CFTR) opening by competing with ATP for a binding site presumably in the COOH-terminal nucleotide binding domain (NBD2). We also found that the open time of the channel is shortened in the presence of ADP. To further study this effect of ADP on the open state, we have used two CFTR mutants (D1370N...
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Two papers, one in this issue (Weinreich et al., 1999) and the other in the April issue of The Journal (Zelt-wanger et al., 1999), help clarify the gating mechanisms of cystic fibrosis transmembrane conductance regulator (CFTR) Cl Ϫ channels, the products of the gene found mutated in cystic fibrosis patients. CFTR is a most unusual ion channel. It is a prominent member of the ABC transporter su...
متن کاملCFTR Gating I
The CFTR chloride channel is activated by phosphorylation of serine residues in the regulatory (R) domain and then gated by ATP binding and hydrolysis at the nucleotide binding domains (NBDs). Studies of the ATP-dependent gating process in excised inside-out patches are very often hampered by channel rundown partly caused by membrane-associated phosphatases. Since the severed DeltaR-CFTR, whose...
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15 صفحه اولModulation of CFTR gating by permeant ions
Cystic fibrosis transmembrane conductance regulator (CFTR) is unique among ion channels in that after its phosphorylation by protein kinase A (PKA), its ATP-dependent gating violates microscopic reversibility caused by the intimate involvement of ATP hydrolysis in controlling channel closure. Recent studies suggest a gating model featuring an energetic coupling between opening and closing of th...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2015
ISSN: 0006-3495
DOI: 10.1016/j.bpj.2014.11.3186