![[ Back to EurekAlert! ]](http://www.eurekalert.org/images/back2e.gif){kind=small}
Public release date: 6-May-2013[ | E-mail |
Share ] Contact: Rita Sullivan King
news@rupress.org
212-327-8603
Rockefeller University Press
A mutant protein responsible for Hutchinson-Gilford Progeria syndrome (HGPS) bars large proteins from entering the nucleus, according to a study in The Journal of Cell Biology.
The culprit in HGPS, a fatal disease that resembles premature aging, is a protein variant called Progerin. This defective protein impairs cells in many ways, including reducing nuclear levels of the RanGTPase. Ran is crucial for nuclear import and export, as it stimulates unloading of cargo that has just entered the nucleus and loading of cargo that's ready to exit. Progerin also impedes the import of Tpr, which forms the basket-like structure on the inner side of nuclear pores. But the mechanism behind this exclusion wasn't clear.
One possibility is that Progerin disrupts the activity of Tpr's nuclear localization sequence (NLS). To test this idea, a team led by researchers from the University of Virginia replaced Tpr's NLS with the localization sequence from a protein that readily enters the nucleus. The modified Tpr was still locked out, however, suggesting that the effect wasn't related to its NLS.
Tpr is one of the largest proteins to traverse nuclear pores. The researchers found that Progerin also limits the nuclear import of three other hefty proteins. This size effect stems from the reduction in nuclear Ran levels triggered by Progerin. For reasons that are still unclear, large cargoes require more Ran to enter the nucleus. These findings suggest that some cellular defects of HGPS might result from the exclusion of large cargoes, such as multisubunit enzyme complexes, from the nucleus.
###
Snow, C.J., et al. 2013. J. Cell Biol. doi:10.1083/jcb.201212117
About The Journal of Cell Biology The Journal of Cell Biology (JCB) is published by The Rockefeller University Press. All editorial decisions on manuscripts submitted are made by active scientists in conjunction with our in-house scientific editors. JCB 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 http://www.jcb.org
[ | E-mail | 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.
Public release date: 6-May-2013[ | E-mail |
Share ] Contact: Rita Sullivan King
news@rupress.org
212-327-8603
Rockefeller University Press
A mutant protein responsible for Hutchinson-Gilford Progeria syndrome (HGPS) bars large proteins from entering the nucleus, according to a study in The Journal of Cell Biology.
The culprit in HGPS, a fatal disease that resembles premature aging, is a protein variant called Progerin. This defective protein impairs cells in many ways, including reducing nuclear levels of the RanGTPase. Ran is crucial for nuclear import and export, as it stimulates unloading of cargo that has just entered the nucleus and loading of cargo that's ready to exit. Progerin also impedes the import of Tpr, which forms the basket-like structure on the inner side of nuclear pores. But the mechanism behind this exclusion wasn't clear.
One possibility is that Progerin disrupts the activity of Tpr's nuclear localization sequence (NLS). To test this idea, a team led by researchers from the University of Virginia replaced Tpr's NLS with the localization sequence from a protein that readily enters the nucleus. The modified Tpr was still locked out, however, suggesting that the effect wasn't related to its NLS.
Tpr is one of the largest proteins to traverse nuclear pores. The researchers found that Progerin also limits the nuclear import of three other hefty proteins. This size effect stems from the reduction in nuclear Ran levels triggered by Progerin. For reasons that are still unclear, large cargoes require more Ran to enter the nucleus. These findings suggest that some cellular defects of HGPS might result from the exclusion of large cargoes, such as multisubunit enzyme complexes, from the nucleus.
###
Snow, C.J., et al. 2013. J. Cell Biol. doi:10.1083/jcb.201212117
About The Journal of Cell Biology The Journal of Cell Biology (JCB) is published by The Rockefeller University Press. All editorial decisions on manuscripts submitted are made by active scientists in conjunction with our in-house scientific editors. JCB 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 http://www.jcb.org
[ | E-mail | 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/2013-05/rup-pm050313.php
Olympus Has Fallen Arnold Palmer Invitational 2013 arnold palmer invitational Chinua Achebe The Croods ashley greene marquette university
No comments:
Post a Comment
Note: Only a member of this blog may post a comment.