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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D O I：

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中图分类号：

学科分类号：

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.

引用

页码：920 / 926

页数：6

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