Search results for: Ying-Chun Yu

Items from 1 to 9 out of 9 results

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Functional stability of CFTR depends on tight binding of ATP at its degenerate ATP‐binding site

Han‐I Yeh, Ying‐Chun Yu, Pei‐Lun Kuo, Chun‐Kuang Tsai, more

The Journal of Physiology > 599 > 20 > 4625 - 4642

Abstract Opening of the cystic fibrosis transmembrane conductance regulator (CFTR) channel is coupled to the motion of its two nucleotide‐binding domains: they form a heterodimer sandwiching two functionally distinct ATP‐binding sites (sites 1 and 2). While active ATP hydrolysis in site 2 triggers rapid channel closure, the functional role of stable ATP binding in the catalysis‐incompetent (or degenerate)...

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Structural mechanisms for defective CFTR gating caused by the Q1412X mutation, a severe Class VI pathogenic mutation in cystic fibrosis

Jiunn‐Tyng Yeh, Ying‐Chun Yu, Tzyh‐Chang Hwang

The Journal of Physiology > 597 > 2 > 543 - 560

Key points Electrophysiological characterization of Q1412X‐CFTR, a C‐terminal truncation mutation of cystic fibrosis transmembrane conductance regulator (CFTR) associated with the severe form of cystic fibrosis (CF), reveals a gating defect that has not been reported previously. Mechanistic investigations of the gating deficit in Q1412X‐CFTR suggest that the reduced open probability in Q1412X‐CFTR...

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On the mechanism of gating defects caused by the R117H mutation in cystic fibrosis transmembrane conductance regulator

Ying‐Chun Yu, Yoshiro Sohma, Tzyh‐Chang Hwang

The Journal of Physiology > 594 > 12 > 3227 - 3244

Key pointsTwo functional abnormalities of cystic fibrosis transmembrane conductance regulator (CFTR), a 25% reduction of the single‐channel conductance (g) and a ∼13‐fold lower open probability (P_o), were found with the R117H mutation that is associated with mild forms of cystic fibrosis.Characterizations of the gating defects of R117H‐CFTR led to the conclusion that the mutation decreases P_o by perturbing...

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Effects of Genistein and Curcumin on Non ATP-Hydrolytic CFTR Mutants

Yumi Nakamura, Akiko Hanyuda, Ying-Chun Yu, Tomoka Hagiya-Furukawa, more

Biophysical Journal > 2012 > 102 > 3 Supplement 1 > 548a

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Curcumin and genistein additively potentiate G551D-CFTR

Ying-Chun Yu, Haruna Miki, Yumi Nakamura, Akiko Hanyuda, more

Journal of Cystic Fibrosis > 2011 > 10 > 4 > 243-252

The G551D mutation in the cystic fibrosis transmembrane conductance regulator (CFTR) is a common cause of cystic fibrosis (CF). G551D-CFTR is characterized by an extremely low open probability despite its normal trafficking to the plasma membrane. Numerous small molecules have been shown to increase the activity of G551D-CFTR presumably by binding to the CFTR protein.We investigated the effect of...

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A hidden Intermediate State for Priming ATP-Hydrolysis During Open Conformation in CFTR Channels

Yoshiro Sohma, Ying-Chun Yu, Masato Yasui, Tzyh-Chang Hwang

Biophysical Journal > 2011 > 100 > 3 Supplement 1 > 263a

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A stable ATP binding to the nucleotide binding domain is important for reliable gating cycle in an ABC transporter CFTR

Hiroyasu Shimizu, Ying-Chun Yu, Koichi Kono, Takahiro Kubota, more

The Journal of Physiological Sciences > 2010 > 60 > 5 > 353-362

Cystic fibrosis transmembrane conductance regulator (CFTR) anion channel, a member of ABC transporter superfamily, gates following ATP-dependent conformational changes of the nucleotide binding domains (NBD). Reflecting the hundreds of milliseconds duration of the channel open state corresponding to the dimerization of two NBDs, macroscopic WT-CFTR currents usually showed a fast, single exponential...