SUMOylation regulates telomere length homeostasis by targeting Cdc13

被引：0
|
作者：
Lisa E Hang
Xianpeng Liu
Iris Cheung
Yan Yang
Xiaolan Zhao
机构：
[1] Molecular Biology Program,Department of Molecular Biology
[2] Memorial Sloan Kettering Cancer Center,undefined
[3] Programs in Biochemistry,undefined
[4] Cell and Molecular Biology,undefined
[5] Weill Graduate School of Medical Sciences,undefined
[6] Cornell University,undefined
[7] Princeton University,undefined
[8] Present addresses: Department of Biochemistry and Molecular Biology,undefined
[9] Louisiana State University,undefined
[10] Health Sciences Center,undefined
[11] Shreveport,undefined
[12] Louisiana,undefined
[13] USA (X.L.); Eurofins MWG Operon,undefined
[14] Huntsville,undefined
[15] Alabama,undefined
[16] USA (I.C.); New York University Medical School,undefined
[17] New York,undefined
[18] New York,undefined
[19] USA (Y.Y.).,undefined
来源：
Nature Structural & Molecular Biology | 2011年 / 18卷
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摘要：
Cdc13 forms a complex with Stn1-Ten1 that caps budding yeast telomeres; Cdc13 also recruits the telomerase complex. Indeed, Cdk1 phosphorylates Cdc13 and this favors the Cdc13- Est1p, at the expense of Cdc13 association with Stn1, which inhibits telomerase action at telomeres. Now a second, independent mechanism to control Cdc13-Stn1 interaction is revealed: sumoylation of Cdc13 promotes its interaction with Stn1 and prevents telomerase activity.
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页码：920 / 926
页数：6
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