Thursday, September 27, 2012

New insights into functionality of cystic fibrosis protein

New insights into functionality of cystic fibrosis protein [ Back to EurekAlert! ] Public release date: 26-Sep-2012
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Contact: Rita Sullivan King
news@rupress.org
212-327-8603
Rockefeller University Press

CFTR is an important protein that, when mutated, causes the life-threatening genetic disease cystic fibrosis. A study in The Journal of General Physiology (JGP) details how an accidental discovery has provided new understanding about CFTR functionality.

From a scientific standpoint, CFTR is unique in that it is the only known ion channela protein pore that enables the passive diffusion of ions across cell membranesin the enormous superfamily of ABC proteins, which normally operate as active transporters. As active transporters, ABC proteins use energy derived from ATP hydrolysis to move substrates across the cell membrane against a concentration gradient. Although CFTR is equipped with the same structural elements as that of its ABC family "brethren," it has been unclear whether the ion channel also functions in the same way.

In the October 2012 issue of JGP, Tzyh-Chang Hwang (University of Missouri-Columbia) and colleagues effectively demonstrate that the mechanism through which CFTR functions is indeed akin to that of the ABC transporters. Specifically, the team used a mutant CFTR channel that exhibits two different open states to determine that ATP hydrolysis underlies the unidirectional cycling of CFTR through its open and closed states. This insight provides new evidence about the functionality of a protein that plays an important role in a very prevalent human disease, and continues to be of great interest to researchers.

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About The Journal of General Physiology (JGP)

Founded in 1918, JGP is published by The Rockefeller University Press. All editorial decisions on manuscripts submitted are made by active scientists. JGP content is posted to PubMed Central, where it is available to the public for free six months after publication. Authors retain copyright of their published works and third parties may reuse the content for non-commercial purposes under a creative commons license. For more information, please visit www.jgp.org.

Jih, K.-Y., et al. 2012. J. Gen. Physiol. 140:347. Tsai, M.-F. 2012. J. Gen. Physiol. doi: 140:343.



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New insights into functionality of cystic fibrosis protein [ Back to EurekAlert! ] Public release date: 26-Sep-2012
[ | E-mail | Share Share ]

Contact: Rita Sullivan King
news@rupress.org
212-327-8603
Rockefeller University Press

CFTR is an important protein that, when mutated, causes the life-threatening genetic disease cystic fibrosis. A study in The Journal of General Physiology (JGP) details how an accidental discovery has provided new understanding about CFTR functionality.

From a scientific standpoint, CFTR is unique in that it is the only known ion channela protein pore that enables the passive diffusion of ions across cell membranesin the enormous superfamily of ABC proteins, which normally operate as active transporters. As active transporters, ABC proteins use energy derived from ATP hydrolysis to move substrates across the cell membrane against a concentration gradient. Although CFTR is equipped with the same structural elements as that of its ABC family "brethren," it has been unclear whether the ion channel also functions in the same way.

In the October 2012 issue of JGP, Tzyh-Chang Hwang (University of Missouri-Columbia) and colleagues effectively demonstrate that the mechanism through which CFTR functions is indeed akin to that of the ABC transporters. Specifically, the team used a mutant CFTR channel that exhibits two different open states to determine that ATP hydrolysis underlies the unidirectional cycling of CFTR through its open and closed states. This insight provides new evidence about the functionality of a protein that plays an important role in a very prevalent human disease, and continues to be of great interest to researchers.

###

About The Journal of General Physiology (JGP)

Founded in 1918, JGP is published by The Rockefeller University Press. All editorial decisions on manuscripts submitted are made by active scientists. JGP content is posted to PubMed Central, where it is available to the public for free six months after publication. Authors retain copyright of their published works and third parties may reuse the content for non-commercial purposes under a creative commons license. For more information, please visit www.jgp.org.

Jih, K.-Y., et al. 2012. J. Gen. Physiol. 140:347. Tsai, M.-F. 2012. J. Gen. Physiol. doi: 140:343.



[ Back to EurekAlert! ] [ | E-mail | Share Share ]

?


AAAS and EurekAlert! are not responsible for the accuracy of news releases posted to EurekAlert! by contributing institutions or for the use of any information through the EurekAlert! system.


Source: http://www.eurekalert.org/pub_releases/2012-09/rup-nii092612.php

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