Abstract:
:Ycf1p function is regulated by casein kinase 2α, Cka1p, via phosphorylation of Ser251. Cka1p-mediated phosphorylation of Ycf1p is attenuated in response to high salt stress. Previous results from our lab suggest a role for Ycf1p in cellular resistance to salt stress. Here, we show that Ycf1p plays an important role in cellular resistance to salt stress by maintaining the cellular redox balance via glutathione recycling. Our results suggest that during acute salt stress increased Sod1p, Sod2p and Ctt1p activity is the main compensatory for the loss in Ycf1p function that results from reduced Ycf1p-dependent recycling of cellular GSH levels.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Paumi CM,Pickin KA,Jarrar R,Herren CK,Cowley STdoi
10.1016/j.febslet.2012.02.010subject
Has Abstractpub_date
2012-03-23 00:00:00pages
847-53issue
6eissn
0014-5793issn
1873-3468pii
S0014-5793(12)00119-6journal_volume
586pub_type
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